|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-381 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 590.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:COG3839 1 MASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPSM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 241 NLFEGRLASGRIHLPGFSIPLSggaleraPGLSAFEGKDVIFGVRPEDLYdsrlPSGASHPTIPGVVKSIEELGSELIVH 320
Cdd:COG3839 240 NLLPGTVEGGGVRLGGVRLPLP-------AALAAAAGGEVTLGIRPEHLR----LADEGDGGLEATVEVVEPLGSETLVH 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 321 LKIDAVRIdsgdpdavedlsgaanaVARFEAVSAVETGQSIDLAIDPAKLHFFHPQTHMAL 381
Cdd:COG3839 309 VRLGGQEL-----------------VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-377 |
4.05e-173 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 486.27 E-value: 4.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPSM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 241 NLFEGRLASGrihlpGFSIPLSGG-ALERAPGLSAFEGKDVIFGVRPEDLydsRLPSGAshPTIPGVVKSIEELGSELIV 319
Cdd:PRK11650 241 NLLDGRVSAD-----GAAFELAGGiALPLGGGYRQYAGRKLTLGIRPEHI---ALSSAE--GGVPLTVDTVELLGADNLA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 320 HLKIDAVRIdsgdpdavedlsgaanaVARFEAVSAVETGQSIDLAIDPAKLHFFHPQT 377
Cdd:PRK11650 311 HGRWGGQPL-----------------VVRLPHQERPAAGSTLWLHLPANQLHLFDADT 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-373 |
4.34e-154 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 437.99 E-value: 4.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:COG3842 3 MPALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGspSM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 241 NLFEGRLASGRihlpGFSIPLSGGALERAPGLSAFEGKDVIFGVRPEDLydsRLPSGASHPTIPGVVKSIEELGSELIVH 320
Cdd:COG3842 240 NLLPGTVLGDE----GGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDI---RLSPEGPENGLPGTVEDVVFLGSHVRYR 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 321 lkidaVRIDSGDPdavedlsgaANAVARFEAVSAVETGQSIDLAIDPAKLHFF 373
Cdd:COG3842 313 -----VRLGDGQE---------LVVRVPNRAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-374 |
5.16e-151 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 430.99 E-value: 5.16e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPSM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 241 NLFEGRLASG-----RIHLPG---FSIPLSGGALERAPGLSafegkdviFGVRPEDLydsrLPSGASHPTIPGVVKSIEE 312
Cdd:PRK11000 240 NFLPVKVTATaieqvQVELPNrqqVWLPVEGRGVQVGANMS--------LGIRPEHL----LPSDIADVTLEGEVQVVEQ 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 313 LGSELIVHLKIDAVRidsgdpdavedlsgaANAVARFEAVSAVETGQSIDLAIDPAKLHFFH 374
Cdd:PRK11000 308 LGNETQIHIQIPAIR---------------QNLVYRQNDVVLVEEGATFAIGLPPERCHLFR 354
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
3.90e-133 |
|
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: 379.29 E-value: 3.90e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVD 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-324 |
9.72e-118 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 345.59 E-value: 9.72e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDkICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV-VDLAPKDRDIA 79
Cdd:COG1118 1 MSIEVRN-ISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPs 239
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 240 mNLFEGRLASGRIHLPGFSIPLSGGALErapglsafegKDVIFGVRPEDLydSRLPSGASHPTIPGVVKSIEELGSELIV 319
Cdd:COG1118 238 -NVLRGRVIGGQLEADGLTLPVAEPLPD----------GPAVAGVRPHDI--EVSREPEGENTFPATVARVSELGPEVRV 304
|
....*
gi 1586515037 320 HLKID 324
Cdd:COG1118 305 ELKLE 309
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-373 |
2.53e-112 |
|
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: 332.00 E-value: 2.53e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIakiLQLEPLLGNK---PAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAEL---LDLVGLPGSErkyPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGs 237
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 238 pSMNLFEGRLASGRIHLPG-FSIPLSGGALERAPGLSAFegkdvifgVRPEDLYDSrlPSGASHPTIPGVVKSIEELGSE 316
Cdd:TIGR03265 237 -EVNWLPGTRGGGSRARVGgLTLACAPGLAQPGASVRLA--------VRPEDIRVS--PAGNAANLLLARVEDMEFLGAF 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 317 LIVHLKIDavridsGDPDA--VEDLSgaANAVARFeavsAVETGQSIDLAIDPAKLHFF 373
Cdd:TIGR03265 306 YRLRLRLE------GLPGQalVADVS--ASEVERL----GIRAGQPIWIELPAERLRAF 352
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
1.54e-111 |
|
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: 324.47 E-value: 1.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVD 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-321 |
1.83e-111 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 330.37 E-value: 1.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVF 82
Cdd:PRK09452 14 LVELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGspSMNL 242
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 243 FEG----RLASGRIhlpgfSIPLSGGALERAPGLSAFEGKDVIFGVRPEDLYDSRLPSGASHPTIPGVVKSIEELGS--E 316
Cdd:PRK09452 251 FDAtvieRLDEQRV-----RANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMtlD 325
|
....*
gi 1586515037 317 LIVHL 321
Cdd:PRK09452 326 SVVEL 330
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
5.07e-111 |
|
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: 324.19 E-value: 5.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-373 |
2.79e-104 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 311.55 E-value: 2.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGN---SYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD-----LAP 73
Cdd:NF040933 1 VTVRVENVTKIFKKgkkEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 74 KDRDIAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 154 AAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAG 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 234 FIGspSMNLFEGRLASGRIHLPG-FSIPLSGGALerapglsafEGKDVIFGVRPEDLYDSRLPSGASHPTI---PGVVKS 309
Cdd:NF040933 241 LIG--DINLLEGKVEEEGLVDGNdLKIPLPNPKL---------EAGEVIIGIRPEDIDISESDMRLPPGFVevgKGRVKV 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 310 IEELGselivhlkidavridsGDPDAVedLSGAANAVARFEAVSA--VETGQSIDLAIDPAKLHFF 373
Cdd:NF040933 310 SSYAG----------------GVFRVV--VSPIDDDSIEIIVNSDrpIEEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-307 |
1.72e-99 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 298.94 E-value: 1.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPsmNLF 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 244 EGRLASGRIHLPGFSIPLSGGAlerAPGLSafEGkDVIFGVRPEDLYDSRLPSGASHPTIPGVV 307
Cdd:PRK11432 244 PATLSGDYVDIYGYRLPRPAAF---AFNLP--DG-ECTVGVRPEAITLSEQGEESQRCTIKHVA 301
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-324 |
1.98e-95 |
|
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: 287.85 E-value: 1.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 35 LVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKR 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 115 VHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 195 QTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGspSMNLFEG----RLASGRIHLPGFSIPLSGGALERAP 270
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIG--EINVFEAtvieRKSEQVVLAGVEGRRCDIYTDVPVE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 271 GlsafeGKDVIFGVRPEDLYDSRLPSGASHPTIPGVVKSIEELGSELIVHLKID 324
Cdd:TIGR01187 239 K-----DQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLE 287
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-237 |
5.15e-90 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 273.12 E-value: 5.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ 83
Cdd:COG1125 4 FENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEP--LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGS 237
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-237 |
4.95e-89 |
|
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: 268.44 E-value: 4.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDkICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAM 80
Cdd:cd03296 1 MSIEVRN-VSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGK----NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
.
gi 1586515037 237 S 237
Cdd:cd03296 239 E 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.67e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 265.03 E-value: 1.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTY---GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlAPKDRD 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV---TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-323 |
2.08e-86 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 265.40 E-value: 2.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVFDNIAF 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIAS 179
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 180 LQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSPsmNLFEGR---LASGRI-HLP 255
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVaekGGEGTIlDTG 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 256 GFSIPLSggalERAPGlsafegkDVIFGVRPEDLYDSRLPSGAS-HPTIPGVVKSIEELGSELIVHLKI 323
Cdd:NF040840 254 NIKIELP----EEKKG-------KVRIGIRPEDITISTEKVKTSaRNEFKGKVEEIEDLGPLVKLTLDV 311
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-236 |
1.45e-84 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 257.04 E-value: 1.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:TIGR00968 1 IEIANISKRFG-SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:TIGR00968 80 HYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-219 |
3.09e-83 |
|
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: 252.78 E-value: 3.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNS---YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPkdrDIAMVF 82
Cdd:cd03293 3 VRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLK---GGVLQQVDTP 219
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarpGRIVAEVEVD 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
3.13e-83 |
|
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: 253.41 E-value: 3.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNsyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-331 |
5.34e-82 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 255.15 E-value: 5.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVFDNI 97
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEI 177
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 178 ASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGspSMNLFEGRLASGR-----I 252
Cdd:PRK11607 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SVNVFEGVLKERQedglvI 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 253 HLPGFSIPlsggaLERAPGLSAFEGKDVIFGVRPEDLYDSRLPSGASHPTIPGVVKSIEELGSELIVHlkidaVRIDSG 331
Cdd:PRK11607 271 DSPGLVHP-----LKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYH-----VRLKSG 339
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
2.99e-81 |
|
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: 248.75 E-value: 2.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEP--LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-296 |
6.39e-80 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 249.23 E-value: 6.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSY 85
Cdd:PRK10851 5 IANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMKLAGK----NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:PRK10851 84 ALFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGspSMN 241
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--EVN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 242 LFEGRLASGRIHLPGFSIPLSggalerapGLSAFEGKDVIFgVRPEDLYDSRLPS 296
Cdd:PRK10851 242 RLQGTIRGGQFHVGAHRWPLG--------YTPAYQGPVDLF-LRPWEVDISRRTS 287
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-235 |
1.48e-72 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 227.14 E-value: 1.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD------RDIAMVFQSYALYPHMT 92
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFI 235
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-213 |
1.51e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 225.69 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYG---NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD- 77
Cdd:COG1136 3 PLLELRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 -----IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVRE 152
Cdd:COG1136 83 lrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 153 PAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQtEALTMGDRVAVLKGGVL 213
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
1.73e-72 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 223.60 E-value: 1.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLA----PKDRDIAMV 81
Cdd:cd03229 3 LKNVSKRYGQK-TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAFSmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:cd03229 82 FQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
4.10e-71 |
|
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: 221.59 E-value: 4.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYG---NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD--- 77
Cdd:cd03255 1 IELKNLSKTYGgggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 ---IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALtMGDRVAVLKGGVL 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-235 |
4.84e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 219.59 E-value: 4.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD------RDIAMVFQSYALYPHMT 92
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:COG4175 122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFI 235
Cdd:COG4175 202 MQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
2.40e-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: 211.77 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIhDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD------LAPKDRDIAMVFQSYALYPHMTVFD 95
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKlaGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586515037 176 EIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVD 217
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-236 |
1.96e-66 |
|
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: 214.72 E-value: 1.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAP------KDRDIAMVFQSYALYPHMT 92
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-236 |
2.45e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 204.99 E-value: 2.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 5 VLDKICKTYGnsyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQS 84
Cdd:COG3840 3 RLDDLTYRYG---DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 YALYPHMTVFDNIAF----SMKLagkNKAERtKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:COG3840 80 NNLFPHLTVAQNIGLglrpGLKL---TAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIG 236
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
2.03e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.60 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD-IAMVF 82
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHR 225
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-217 |
3.23e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 201.43 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 158 MDEPLSNLDAklrvQMRAEIASL-QR--QLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVD 217
Cdd:COG2884 161 ADEPTGNLDP----ETSWEIMELlEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-328 |
2.50e-61 |
|
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: 201.10 E-value: 2.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD------LAPKDRDIAMVFQSYALYPHMTVFD 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKLAGKnkAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:COG4148 97 NLLYGRKRAPR--AERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 176 EIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGfiGSPSMNLFEGRLASgriHLP 255
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAA---HDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 256 GF---SIPLSGGALeRAPGLSAFEGKDVIFGVRPEDLYDSRlpsgaSHPT-------IPGVVKSIEEL-GSELIVHLKID 324
Cdd:COG4148 250 DYgltRLALGGGRL-WVPRLDLPPGTRVRVRIRARDVSLAL-----EPPEgssilniLPGRVVEIEPAdGGQVLVRLDLG 323
|
....
gi 1586515037 325 AVRI 328
Cdd:COG4148 324 GQTL 327
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-226 |
1.05e-60 |
|
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: 203.98 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYG----NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--- 75
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 76 --RDIAMVFQ--SYALYPHMTVFDNIAFSMKLAGK-NKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAM 149
Cdd:COG1123 340 lrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
4.01e-59 |
|
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: 191.39 E-value: 4.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQsyalYP-----HMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-235 |
4.02e-59 |
|
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: 191.73 E-value: 4.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD---- 77
Cdd:COG1127 4 PMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 -IAMVFQSYALYPHMTVFDNIAFSMK-LAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:COG1127 83 rIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 156 FLMDEPLSNLD---AKLRVQMraeIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPvNAFVA 232
Cdd:COG1127 163 LLYDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVR 238
|
...
gi 1586515037 233 GFI 235
Cdd:COG1127 239 QFL 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-237 |
6.98e-59 |
|
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: 191.17 E-value: 6.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYH---AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDI 78
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQSY--ALYPHMTVFDNIAFSMKLAGKnkAERTKRVHEIAKILQLEP-LLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFI 235
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELL 239
|
..
gi 1586515037 236 GS 237
Cdd:COG1124 240 AA 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-226 |
1.33e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.21 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDvVDLAPKD-----RD 77
Cdd:COG1126 1 MIEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED-LTDSKKDinklrRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFS-MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 157 LMDEPLSNLDAklrvQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG1126 159 LFDEPTSALDP----ELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
8.81e-58 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 187.29 E-value: 8.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 5 VLDKICKTYGNSYH-AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQsyalYP-HM----TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-213 |
9.08e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.44 E-value: 9.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTY---GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD 77
Cdd:COG1135 4 LENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 158 MDEPLSNLDAK-----LRVqmraeIASLQRQLGVTTIYVTHDqtealtMG------DRVAVLKGGVL 213
Cdd:COG1135 164 CDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRI 219
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-228 |
1.07e-57 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 188.41 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNS---YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPkDRdiAM 80
Cdd:NF040729 2 LKIQNISKTFINNkkeNEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-DR--GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVL---KGGVLQQVdtpKALYHRPVN 228
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrdKGKILEDL---KIDLPRPRN 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-213 |
3.33e-57 |
|
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: 186.63 E-value: 3.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGN---SYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD---- 75
Cdd:cd03258 1 MIELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 76 -RDIAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-211 |
3.87e-56 |
|
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: 183.48 E-value: 3.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-----DIAM 80
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSY--ALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEP---LLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:cd03257 87 VFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
5.03e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 181.98 E-value: 5.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSY---HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdLAPkDRD 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGP-GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-211 |
9.71e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.94 E-value: 9.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----R 76
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 77 DIAMVFQSYALYPHMTVFDNIafsmkLAGK--------------NKAERtKRVHEIAKILQLEPLLGNKPAQLSGGQRQR 142
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNV-----LAGRlgrtstwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 143 VAMGRAMVREPAAFLMDEPLSNLDAKL-RVQMRAeIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
1.95e-53 |
|
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: 176.92 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAM 80
Cdd:cd03261 3 LRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGK-NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-213 |
4.81e-53 |
|
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: 175.03 E-value: 4.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV----VDLAPKDRDIAMVFQSYA 86
Cdd:cd03262 8 KSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 87 LYPHMTVFDNIAFS-MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:cd03262 87 LFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 166 DAklrvQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03262 167 DP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-226 |
9.51e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 180.10 E-value: 9.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS---SGTLSIGGQDVVDLAPKDR--DIAMVFQS--YALYPh 90
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQLNP- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:COG1123 99 VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 171 VQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG1123 179 AEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-211 |
1.47e-51 |
|
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: 171.14 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnsyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQ 83
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-211 |
3.79e-51 |
|
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: 170.12 E-value: 3.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD 77
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-222 |
4.79e-51 |
|
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: 170.81 E-value: 4.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-DIAMVFQSYALYP 89
Cdd:COG4555 9 KKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 170 RVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:COG4555 168 RRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-216 |
3.48e-50 |
|
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: 167.73 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 15 NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVF 94
Cdd:TIGR01277 9 EYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMR 174
Cdd:TIGR01277 89 QNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586515037 175 AEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQV 216
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
6.72e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 6.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHaIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ 83
Cdd:COG4619 3 LEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPhMTVFDNIAFSMKLagKNKAERTKRVHEIAKILQLEPLLGNKPA-QLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQL--RERKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-235 |
8.22e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.88 E-value: 8.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 8 KICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDI----AMVFQ 83
Cdd:PRK09493 6 NVSKHFGPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFS-MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:PRK09493 85 QFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 163 SNLDAKLrvqmRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFI 235
Cdd:PRK09493 165 SALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
2.31e-48 |
|
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: 162.96 E-value: 2.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 159 DEPLSNLDAklrvQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03292 161 DEPTGNLDP----DTTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-234 |
7.52e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 167.13 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD------RDIAMVFQSYALYPHMT 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGF 234
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-222 |
9.90e-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: 9.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ 83
Cdd:COG1120 4 AENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFS----MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:COG1120 83 EPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-217 |
1.05e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 162.11 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdVVDLA----PKD-----R 76
Cdd:PRK11124 5 LNGINCFYG-AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN-HFDFSktpsDKAirelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 77 DIAMVFQSYALYPHMTVFDN-IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQrQLGVTTIYVTHDQTEALTMGDRVAVL-KGGVLQQVD 217
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMeNGHIVEQGD 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-226 |
2.25e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 163.75 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAMVFQ-SYA-LYPH 90
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAG-KNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDak 168
Cdd:COG4608 112 MTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 169 lrVQMRAEI----ASLQRQLGVTTIYVTHDqteaLTM----GDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG4608 190 --VSIQAQVlnllEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-217 |
4.52e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvDLAPK---------DR 76
Cdd:COG4161 5 LKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKpsekairllRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 77 DIAMVFQSYALYPHMTVFDN-IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQrQLGVTTIYVTHDQTEALTMGDRVAVL-KGGVLQQVD 217
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMeKGRIIEQGD 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-211 |
7.32e-47 |
|
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: 160.04 E-value: 7.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAM 80
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSM--------KLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVRE 152
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 153 PAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-312 |
1.26e-46 |
|
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: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGG---QDV---VDLAPKDRDIAMVFQSYALYPHMTVFD 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSrkgIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKLAgkNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:TIGR02142 95 NLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 176 EIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAgfiGSPSMNLFEGRLASGRIHLP 255
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQGSLIEGVVAEHDQHYG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 256 GFSIPLSGGALErAPGLSAFEGKDVIFGVRPEDLYDSRLPSGASHPT--IPGVVKSIEE 312
Cdd:TIGR02142 250 LTALRLGGGHLW-VPENLGPTGARLRLRVPARDVSLALQKPEATSIRniLPARVVEIED 307
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-211 |
2.12e-46 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 158.40 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPkdrDIAMVFQSYALYPHMTVFDNIAF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMK--LAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEI 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 1586515037 178 ASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-202 |
2.92e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 157.26 E-value: 2.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL--EEIS-SGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVFDN 96
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKlAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAE 176
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180
....*....|....*....|....*.
gi 1586515037 177 IASLQRQLGVTTIYVTHDQTEALTMG 202
Cdd:COG4136 176 VFEQIRQRGIPALLVTHDEEDAPAAG 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-211 |
3.10e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 158.69 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGqdvVDLAPKDRDIAMVFQ 83
Cdd:PRK11247 13 LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGKNKAertkrvHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLKGQWRDAA------LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
5.91e-46 |
|
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: 155.25 E-value: 5.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-DIAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIafsmklagknkaertkrvheiakilqlepllgnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-213 |
1.79e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.20 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTY---GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD 77
Cdd:PRK11153 4 LKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDqtealtMG------DRVAVLKGGVL 213
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHE------MDvvkricDRVAVIDAGRL 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-222 |
2.00e-45 |
|
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: 155.80 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEI-----SSGTLSIGGQDVVDLAPKD----RDIAMVFQ 83
Cdd:cd03260 10 YGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRRVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPhMTVFDNIAFSMKLAG-KNKAERTKRVHEIAKILQLEPLLGNK--PAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:cd03260 89 KPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQlgVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
2.96e-45 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 155.28 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNSYHAI---KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvDLAPKDRD- 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELtilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 --------IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAErtKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:COG4181 84 rarlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALtMGDRVAVLKGGVLQQVDTPKA 221
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-226 |
1.53e-44 |
|
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: 156.37 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE---ISSGTLSIGGQDVVDLAPKD------RDIAMV 81
Cdd:COG0444 12 PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQ-SY-ALYPHMTVFDNIAFSMKLAGK-NKAERTKRVHEIAKILQLEP---LLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:COG0444 92 FQdPMtSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
1.68e-43 |
|
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: 150.35 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSY-HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV-DLAPKDRDIAMV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKPA-QLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRArTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQLGVttIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-223 |
1.77e-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 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: 152.22 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 15 NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAMVFQsyalYP 89
Cdd:TIGR04521 16 FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HM-----TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:TIGR04521 92 EHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-211 |
2.27e-42 |
|
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: 148.22 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNI--------AFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
6.56e-42 |
|
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: 144.45 E-value: 6.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYH-AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYpHMTVFDNIafsmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDqTEALTMGDRVAVLKGG 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 ... |
6-205 |
8.44e-42 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 145.45 E-value: 8.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RD-IA 79
Cdd:TIGR03608 1 LKNISKKFGDK-VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586515037 160 EPLSNLDAKlrvqMRAEIASLQRQL---GVTTIYVTHDqTEALTMGDRV 205
Cdd:TIGR03608 160 EPTGSLDPK----NRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADRV 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-211 |
9.85e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 9.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYgnsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSY 85
Cdd:PRK10771 4 LTDITWLY---HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-211 |
6.27e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 144.84 E-value: 6.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPkdrDIAMVFQSY 85
Cdd:PRK11248 4 ISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
1.53e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.31 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlAPKDRDIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPH--MTVFDNIAF----SMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL-----QQVDTPKAL---YHRP 226
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPENLsraYGGP 238
|
....*..
gi 1586515037 227 VNAFVAG 233
Cdd:COG1121 239 VALLAHG 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-220 |
2.13e-40 |
|
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: 143.72 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTY-GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlaPKD-----RDIA 79
Cdd:TIGR04520 3 VENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENlweirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSyalyPH-----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALtMGDRVAVLKGGVLQQVDTPK 220
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPR 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-205 |
2.29e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 141.85 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNsyHAI-KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK-DRDIA 79
Cdd:COG4133 1 MMLEAENLSCRRGE--RLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVFDNIAFSMKLAGKNKAERtkRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 160 EPLSNLDAklrvQMRAEIASL---QRQLGVTTIYVTHDQTEA-----LTMGDRV 205
Cdd:COG4133 157 EPFTALDA----AGVALLAELiaaHLARGGAVLLTTHQPLELaaarvLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
3.33e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.69 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ 83
Cdd:cd00267 2 IENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 syalyphmtvfdniafsmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
5.53e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 138.93 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHMTVFDNI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNKAERTKRVHEIAKILQLEPL----LGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
1.39e-39 |
|
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: 149.21 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTY-GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAM 80
Cdd:COG2274 474 IELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYpHMTVFDNIAFSMKLAGKnkaertKRVHEIAKILQLEP-----------LLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLGDPDATD------EEIIEAARLAGLHDfiealpmgydtVVGEGGSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDqTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-211 |
1.24e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.05 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAMVFQSY--ALYPHMT 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMK-LAGKNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586515037 171 VQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-222 |
1.28e-38 |
|
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: 137.57 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAMVFQSYALYP 89
Cdd:cd03224 10 YGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIAFSMKLAGKNKAERTkrvheIAKILQLEPLLGNKPAQ----LSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKAR-----LERVYELFPRLKERRKQlagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 166 DAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03224 164 APKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-213 |
1.88e-38 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 137.11 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGN---SYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlAPKD--RDI 78
Cdd:cd03266 2 ITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 159 DEPLSNLDAKLRVQMRaEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03266 161 DEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-218 |
1.98e-38 |
|
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: 138.40 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAMVFQ-SY-ALYPHMTVF 94
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIAFSMK-LAGKNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:TIGR02769 109 QIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG-VLQQVDT 218
Cdd:TIGR02769 189 ILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEECDV 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-226 |
3.04e-38 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 139.84 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-----DIAMVFQS--YALYPHM 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIA-----FSMKLAgknKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK15079 116 TIGEIIAeplrtYHPKLS---RQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-213 |
3.32e-38 |
|
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: 135.26 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSyalyph 90
Cdd:cd03214 9 YGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQA------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 mtvfdniafsMKLAG-KNKAERtkRVHEiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:cd03214 82 ----------LELLGlAHLADR--PFNE-----------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586515037 170 RVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-208 |
7.39e-38 |
|
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: 136.03 E-value: 7.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAMVFQSY 85
Cdd:cd03219 6 LTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNI----------AFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:cd03219 85 RLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVL 208
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-222 |
1.11e-37 |
|
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: 135.19 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK-DRDIAMVF 82
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-222 |
2.10e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.23 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYpHMTVFDNIAFsmklaGKNKAERtKRVHEIAKILQLEPLLGNKP-----------AQLSGGQRQRVAMGRAMV 150
Cdd:COG1132 420 PQDTFLF-SGTIRENIRY-----GRPDATD-EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 151 REPAAFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-213 |
3.08e-37 |
|
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: 134.02 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 7 DKICKTY---GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR------D 77
Cdd:TIGR02211 5 ENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMgDRVAVLKGGVL 213
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-226 |
3.16e-37 |
|
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: 140.98 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEiSSGTLSIGGQDVVDLAPKD-----RDIAMVFQS-YA-LYPH 90
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKL--AGKNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:COG4172 379 MTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 168 KLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG-VLQQVDTpKALYHRP 226
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGkVVEQGPT-EQVFDAP 517
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
2.41e-36 |
|
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: 138.74 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALyPHMTVFDNIAFSMKLAGK---NKAERTKRVHEIAKILQ--LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG4988 417 PQNPYL-FAGTIRENLRLGRPDASDeelEAALEAAGLDEFVAALPdgLDTPLGEGGRGLSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDqTEALTMGDRVAVLKGGVLQQVDTPKALYHR 225
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-213 |
4.55e-35 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 128.10 E-value: 4.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPH 90
Cdd:cd03268 8 KTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAGKNKaertKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:cd03268 87 LTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586515037 171 VQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03268 163 KELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-225 |
4.84e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 129.85 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 17 YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV--DLAPKDRDIAMVFQSyalyPH---- 90
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQN----PDnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 -MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:PRK13650 96 gATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 170 RVQMRAEIASLQRQLGVTTIYVTHDQTEaLTMGDRVAVLKGGVLQQVDTPKALYHR 225
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-211 |
5.86e-35 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 127.69 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSyHAIKDLSLTIHDGeFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD-IAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRaeiaSLQRQLGVTTIYV--THDQTEALTMGDRVAVLKGG 211
Cdd:cd03264 159 AGLDPEERIRFR----NLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-220 |
7.23e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 7.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSyalyPH- 90
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 ----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK13635 93 qfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 167 AKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTmGDRVAVLKGGVLQQVDTPK 220
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-213 |
7.24e-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: 127.65 E-value: 7.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 12 TYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlapKDRDIAMVFQSYAL---Y 88
Cdd:cd03235 8 SYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSIdrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 89 PhMTVFDNIAF----SMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:cd03235 84 P-ISVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 165 LDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03235 163 VD----PKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-215 |
8.79e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.01 E-value: 8.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 7 DKICKTY--GN-SYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAP------KDRD 77
Cdd:PRK11629 9 DNLCKRYqeGSvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMgDRVAVLKGGVLQQ 215
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-237 |
2.86e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 127.22 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDkICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV-------DLAPK 74
Cdd:COG4598 8 ALEVRD-LHKSFG-DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 75 DRD--------IAMVFQSYALYPHMTVFDNIAFS-MKLAGKNKAErtkrVHEIAKILqLEPL-LGNK----PAQLSGGQR 140
Cdd:COG4598 86 DRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAE----AIERAEAL-LAKVgLADKrdayPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 141 QRVAMGRAMVREPAAFLMDEPLSNLDAKLrVQmraEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVD 217
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
250 260
....*....|....*....|
gi 1586515037 218 TPKALYHRPVNAFVAGFIGS 237
Cdd:COG4598 237 PPAEVFGNPKSERLRQFLSS 256
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-237 |
3.67e-34 |
|
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: 126.87 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV-------DLAPKD- 75
Cdd:TIGR03005 1 VRFSDVTKRFGI-LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngPLVPADe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 76 -------RDIAMVFQSYALYPHMTVFDNIAFS-MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGR 147
Cdd:TIGR03005 80 khlrqmrNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 148 AMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPV 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
250
....*....|
gi 1586515037 228 NAFVAGFIGS 237
Cdd:TIGR03005 240 EERTREFLSK 249
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-226 |
4.74e-34 |
|
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: 125.86 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAMVFQSYALYP 89
Cdd:COG0410 13 YGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIafsmKLAGKNKAERTKRVHEIAKILQLEPLLG---NKPA-QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:COG0410 92 SLTVEENL----LLGAYARRDRAEVRADLERVYELFPRLKerrRQRAgTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 166 DAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG0410 168 APLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-236 |
7.48e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 126.11 E-value: 7.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS-----SGTLSIGGQDV----VDLAPKDRDIAMVFQ 83
Cdd:PRK14267 14 YGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspdVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAG--KNKAERTKRVHEIAKILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLgvTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNA----FVAG 233
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEltekYVTG 250
|
...
gi 1586515037 234 FIG 236
Cdd:PRK14267 251 ALG 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-223 |
8.76e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.70 E-value: 8.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDI----AMVFQ--SYALYPHmT 92
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQL--EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 171 VQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-223 |
2.65e-33 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 124.19 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPhMTVFDNI 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFsmklaGKNKA-----ERTKRVHEIAKIL-----QLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:cd03249 98 RY-----GKPDAtdeevEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 168 K--LRVQmraeiASLQR-QLGVTTIYVTHDQTeALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:cd03249 173 EseKLVQ-----EALDRaMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-211 |
3.03e-33 |
|
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: 123.14 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGqdvVDLAPKDR--DIAMVFQ 83
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 S--YALYPHmTVFDNIAFSMKLAGKNKAertkRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLKELDAGNE----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
2.61e-32 |
|
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: 127.57 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTY-GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDI 78
Cdd:COG4987 332 PSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQSYALYpHMTVFDNIafsmKLAGKNKAERtkRVHEIAKILQLEPLLGNKP-----------AQLSGGQRQRVAMGR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENL----RLARPDATDE--ELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 148 AMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDQTeALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-211 |
3.67e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.73 E-value: 3.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTY----GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR--DIA 79
Cdd:COG1101 4 LKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYAL--YPHMTVFDNIAFSMK------LA-GKNKAERtKRVHEIAKILQ--LEPLLGNKPAQLSGGQRQRVAMGRA 148
Cdd:COG1101 84 RVFQDPMMgtAPSMTIEENLALAYRrgkrrgLRrGLTKKRR-ELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 149 MVREPAAFLMDEPLSNLDAKlrvqMRAEIASLQRQL----GVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-226 |
4.31e-32 |
|
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: 126.72 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKS-TAL---RMIAGLEEISSGTLSIGGQDVVDLAPKD------RDIAMVFQ--SY 85
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQepMT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMKL-AGKNKAERTKRVHEI---AKILQLEPLLGNKPAQLSGGQRQRV--AMgrAMVREPAAFLMD 159
Cdd:COG4172 104 SLNPLHTIGKQIAEVLRLhRGLSGAAARARALELlerVGIPDPERRLDAYPHQLSGGQRQRVmiAM--ALANEPDLLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDqteaLT----MGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
4.65e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.17 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS-----SGTLSIGGQDV--VDLAP 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfkMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 74 KDRDIAMVFQSYALYPHMTVFDNIAFSMKL--AGKNKAERTKRVHEIAKILQL----EPLLGNKPAQLSGGQRQRVAMGR 147
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 148 AMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLgvTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-226 |
4.99e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTAL----RMIaglEEIS----SGTLSIGGQDV----VDLAPKDRDIAM 80
Cdd:COG1117 21 YGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMN---DLIPgarvEGEILLDGEDIydpdVDVVELRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPhMTVFDNIAFSMKLAG-KNKAERTKRVH----------EIAKILqlepllgNKPAQ-LSGGQRQRVAMGRA 148
Cdd:COG1117 97 VFQKPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEeslrkaalwdEVKDRL-------KKSALgLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 149 MVREPAAFLMDEPLSNLD--AKLRVqmraE--IASLQRQlgVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYH 224
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpiSTAKI----EelILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
..
gi 1586515037 225 RP 226
Cdd:COG1117 243 NP 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-226 |
5.04e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.15 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlAPKD------RDIAMVFQS-YA-LYP 89
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEaqkllrQKIQIVFQNpYGsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIAFSMKLAGK-NKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:PRK11308 108 RKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 168 KLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLK-GGVLQQVDTpKALYHRP 226
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYlGRCVEKGTK-EQIFNNP 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-235 |
6.64e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDI------------ 78
Cdd:PRK10619 13 KRYG-EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 ---AMVFQSYALYPHMTVFDNIAFS-MKLAGKNKAE-RTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREP 153
Cdd:PRK10619 92 trlTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEaRERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 154 AAFLMDEPLSNLDAKLrvqmRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAF 230
Cdd:PRK10619 172 EVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
....*
gi 1586515037 231 VAGFI 235
Cdd:PRK10619 248 LQQFL 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-211 |
9.07e-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: 119.96 E-value: 9.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAMVF 82
Cdd:cd03218 3 AENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRAEIASL-QRQLGvttIYVT-HDQTEALTMGDRVAVLKGG 211
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEG 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-214 |
9.72e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 119.31 E-value: 9.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvDLAPKDRdIAMVFQSYALY 88
Cdd:cd03269 6 VTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 89 PHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:cd03269 83 PKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 169 LRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG--VLQ 214
Cdd:cd03269 163 NVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGraVLY 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
1.12e-31 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 117.53 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD---RDIAM 80
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQsyalyphmtvfdniafsmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-211 |
2.89e-31 |
|
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: 118.08 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYpHMTVFD 95
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKLAgknkaeRTKRVHEIAKILQLEPLLGNKP-----------AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:cd03245 97 NITLGAPLA------DDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 165 LDaklrvqMRAE---IASLQRQL-GVTTIYVTHdQTEALTMGDRVAVLKGG 211
Cdd:cd03245 171 MD------MNSEerlKERLRQLLgDKTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-220 |
4.02e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 123.76 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIG-GQDVVDLAPKDRD--------IAMVFQSYALYP 89
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDgrgrakryIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIAFSMKLAGKNKAERTKRVHEIAKI----LQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDELARMKAVITLKMVgfdeEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPK 220
Cdd:TIGR03269 459 DPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-211 |
8.40e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.68 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLapkDRD---------IAMVFQSYALYPH 90
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL---DADalaqlrrehFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:PRK10535 101 LTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586515037 171 VQMRAEIASLQRQlGVTTIYVTHDQTEAlTMGDRVAVLKGG 211
Cdd:PRK10535 181 EEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDG 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-219 |
9.99e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.49 E-value: 9.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:COG4604 2 IEIKNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAF-----SmklAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQR--VAMgrAMVREPA 154
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrfpyS---KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-210 |
1.02e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLS---LTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR------DIAMV 81
Cdd:PRK10584 14 KSVGQGEHELSILTgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:PRK10584 94 FQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKG 210
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-213 |
2.17e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.13 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAM 80
Cdd:PRK10908 4 FEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRqLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
2.86e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.39 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYgNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV---VDLAPKDRD 77
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 I-------AMVFQSYALYPHMTVFDN-IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:PRK11264 80 IrqlrqhvGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-222 |
6.20e-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: 115.02 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYpHMTVFDNIAFSMKLAGKN---KAERTKRVHEiaKILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRPDATDEeviEAAKAAQIHD--KIMRFpdgyDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDQTEALTmGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-211 |
7.48e-30 |
|
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: 115.18 E-value: 7.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSG-TLSI-----GGQDVVDLAPK 74
Cdd:COG1119 1 DPLLELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 75 drdIAMVfqSYAL----YPHMTVFDNI--AF--SMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMG 146
Cdd:COG1119 80 ---IGLV--SPALqlrfPRDETVLDVVlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 147 RAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-213 |
8.30e-30 |
|
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: 112.69 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 5 VLDKICKTYGNSYHAI-KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMV 81
Cdd:cd03246 2 EVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHmTVFDNIafsmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 162 LSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHdQTEALTMGDRVAVLKGGVL 213
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-211 |
8.34e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 117.67 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 37 GPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD------LAPKDRDIAMVFQSYALYPHMTVFDNIAFSMKlaGKNKAE 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 111 RTKrvheIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIY 190
Cdd:PRK11144 109 FDK----IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180
....*....|....*....|.
gi 1586515037 191 VTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQG 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
8.57e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 8.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIG------GQDVVDLAPKDRDIAMVFQsyalYP-HM 91
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKPLRKKVGIVFQ----FPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 ----TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 167 AKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-208 |
1.90e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 118.93 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 12 TYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYP 89
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HmTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQ-----LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:TIGR02857 410 G-TIAENIRLARPDASDAEIREALERAGLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586515037 165 LDAKLRVQMRAEIASLQRqlGVTTIYVTHDqTEALTMGDRVAVL 208
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
2.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNSYH-AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDI 78
Cdd:PRK13632 6 VMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQSyalyPH-----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREP 153
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 154 AAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALtMGDRVAVLKGGVLQQVDTPK 220
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-211 |
2.89e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.82 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvDLAPKDRD-IAmv 81
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRrIG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 fqsY-----ALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG4152 75 ---YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 157 LMDEPLSNLD---AKLrvqMRAEIASLQRQlGVTTIYVTH--DQTEALTmgDRVAVLKGG 211
Cdd:COG4152 152 ILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKG 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-220 |
5.14e-29 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 118.82 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYpHM 91
Cdd:TIGR03375 475 GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSMKLAGK----NKAERTKrVHEIAKILQ--LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:TIGR03375 554 TLRDNIALGAPYADDeeilRAAELAG-VTEFVRRHPdgLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 166 DaklrvqMRAE---IASLQRQL-GVTTIYVTHdQTEALTMGDRVAVLKGG----------VLQQVDTPK 220
Cdd:TIGR03375 633 D------NRSEerfKDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGrivadgpkdqVLEALRKGR 694
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-211 |
5.59e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-RD-- 77
Cdd:COG1129 2 EPLLEMRGISKSFGGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGK---NKAERTKRVHEIAKILQLE--P--LLGNkpaqLSGGQRQRVAMGRAMV 150
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDidPdtPVGD----LSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 151 REPAAFLMDEPLSNLDAK-----LRVqmraeIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG1129 157 RDARVLILDEPTASLTEReverlFRI-----IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-222 |
6.04e-29 |
|
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: 112.32 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMVFQSYALYPH 90
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrdISRKSLRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 mTVFDNIAFSMKLAGK---NKAERTKRVHEIAKILQ--LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:cd03254 92 -TIMENIRLGRPNATDeevIEAAKEAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 166 DAKLRVQMRAEIASLQRqlGVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03254 171 DTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-211 |
1.11e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 111.66 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLA-------- 72
Cdd:COG1137 1 MMTLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 73 ----PKDrdiAMVFQsyalypHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRA 148
Cdd:COG1137 80 igylPQE---ASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 149 MVREPAAFLMDEPLSNLDAKLRVQMRAEIASL-QRQLGVttiYVT-HDQTEALTMGDRVAVLKGG 211
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLkERGIGV---LITdHNVRETLGICDRAYIISEG 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-221 |
1.88e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.96 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHmTVFDNIAF 99
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMKLAGKnKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIAS 179
Cdd:PRK10247 104 PWQIRNQ-QPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586515037 180 LQRQLGVTTIYVTHDQTEaLTMGDRVAVLK--GGVLQQVDTPKA 221
Cdd:PRK10247 183 YVREQNIAVLWVTHDKDE-INHADKVITLQphAGEMQEARYELA 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-215 |
4.18e-28 |
|
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: 115.62 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHmTVFDNI 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 A-FSM----------KLAGknkaertkrVHEIakILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:COG4618 427 ArFGDadpekvvaaaKLAG---------VHEM--ILRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 163 SNLDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTeALTMGDRVAVLKGGVLQQ 215
Cdd:COG4618 496 SNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-213 |
6.27e-28 |
|
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: 109.16 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 17 YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLapkdrDIAMVFQsyalyPHMTVFDN 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKP-AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586515037 176 EIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
7.45e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.14 E-value: 7.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQ------DV--VDLAPKDRDIAMVFQS 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIfqIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 YALYPHMTVFDNIAFSMKLAG-KNKAERTKRVHEIAKIL----QLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQlgVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFI 235
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-215 |
7.89e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 109.24 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAI-KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYpHMTVFDNIAFSMKLAGKNKAERTKRV---HEIAKIL--QLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAanaHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHDQTeALTMGDRVAVL-KGGVLQQ 215
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLeDGKIVER 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-228 |
9.01e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS-----SGTLSIGGQDV----VDLAPKDRDIAMVFQ 83
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPhMTVFDNIAFSMKLAG-KNKAERTKRVHEI---AKIL-QLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSlkgASIWdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRQLgvTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVN 228
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-225 |
2.70e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTA----LRMIAgleeiSSGTLSIGGQDVVDLAPKD-----RDIAMVFQ--SYA 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 87 LYPHMTVFDNIAFSMKLAGK--NKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG-VLQQVD------TPKALYHR 225
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQGDcervfaAPQQEYTR 523
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-229 |
4.22e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISS-----GTLSIGGQDV----VDLAPKDRDIAMVFQ 83
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPhMTVFDNIAFSMKLAG-KNKAERTKRVHEIAKILQLEPLLGNK----PAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKG-----GVLQQVDTPKALYHRPVNA 229
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDS 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-226 |
1.18e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.49 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKS-TALRMIAGLEEiSSGTLSIGG-------QDVVDLAPKDR---------DIAMV 81
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsRQVIELSEQSAaqmrhvrgaDMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQS--YALYPHMTVFDNIAFSMKL---AGKNKAER-TKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLhqgASREEAMVeAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-211 |
2.10e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-RD--IA 79
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVFDNIAFSM---KLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 157 LMDEPLSNL-----DAKLRV--QMRAEiaslqrqlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG3845 164 ILDEPTAVLtpqeaDELFEIlrRLAAE--------GKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-214 |
3.90e-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: 104.72 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-RDIAMVF-QSYALYPHMTVFDN 96
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKPA-QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELL-DTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586515037 176 EIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQ 214
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-226 |
4.81e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.56 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLA-----PKDRDIAMVFQS-YA-LYPH 90
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAGKNKAERT-KRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 169 LRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-223 |
6.28e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 17 YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD------LAPKDRDIAMVFQsyalYPH 90
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVF-DNIAFSMKLAGKNKAERTKRVHEIAKILQLE-----PLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK13646 96 SQLFeDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 165 LDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-211 |
7.38e-26 |
|
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: 103.76 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAMVF 82
Cdd:TIGR03410 3 VSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQlePLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-213 |
9.94e-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: 102.63 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL--EEISSGTLSIGGQDVVDLAPKDRdIAMVFQSYALYPHMTVFDNI 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlrvqMRAEI 177
Cdd:cd03213 104 MFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS----SALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586515037 178 ASLQRQL---GVTTIYVTHD-QTEALTMGDRVAVL-KGGVL 213
Cdd:cd03213 151 MSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLsQGRVI 191
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-214 |
1.39e-25 |
|
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: 108.20 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHmTVFDNI 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNK---AERTKRVHEIakILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:TIGR01842 413 ARFGENADPEKiieAAKLAGVHEL--ILRLpdgyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586515037 171 VQMRAEIASLQRQlGVTTIYVTHdQTEALTMGDRVAVLKGGVLQ 214
Cdd:TIGR01842 491 QALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIA 532
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
2.15e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLaPKDR---- 76
Cdd:PRK11614 3 KVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKimre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 77 DIAMVFQSYALYPHMTVFDNIAFsmklaGKNKAERTKRVHEIAKILQLEPLLGNKPAQ----LSGGQRQRVAMGRAMVRE 152
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 153 PAAFLMDEPLSNLDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-226 |
3.95e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK--DRDIAMVFQSYALYPHmTVFDNI 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNK---AERTKRVHE-IAKILQ-LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAklrvQ 172
Cdd:TIGR00958 576 AYGLTDTPDEEimaAAKAANAHDfIMEFPNgYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----E 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:TIGR00958 652 CEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-223 |
4.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV--DLAPKDRDIAMVFQSY-ALYPHMTVFDN 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAE 176
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586515037 177 IASLQRQLGVTTIYVTHDQTEALTmGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-222 |
9.71e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPH 90
Cdd:PRK11231 12 YGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFS----MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK11231 91 ITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 167 aklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL------QQVDTPKAL 222
Cdd:PRK11231 171 ----INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVmaqgtpEEVMTPGLL 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-256 |
1.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV------DLAPKDRDIAMVFQsyalYPHMTVFD 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 N-----IAFSMKLAGKNKAE-RTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:PRK13641 101 NtvlkdVEFGPKNFGFSEDEaKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 170 RVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPvNAFVAGFIGSPSMNLFEGRLAS 249
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSRFASKLEK 258
|
....*..
gi 1586515037 250 GRIHLPG 256
Cdd:PRK13641 259 GGFKFSE 265
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-229 |
1.63e-24 |
|
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: 100.14 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE----ISSGTLSIGGQDVVDLAPKDRDIAMVFQS--YALYPHMT 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKR-VHEIAKI--LQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALiLEALEAVglPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 170 RVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNA 229
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-229 |
1.63e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdVVDLApkdrDIAMVFQsyalyPH 90
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALL----ELGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 170 RVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPK---ALYHRPVNA 229
Cdd:COG1134 182 QKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEeviAAYEALLAG 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-213 |
1.97e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.04 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEiSSGTLSigGQDVVDLAPKDRD-----IAMVFQSYALYPHMTVF 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTS--GQILFNGQPRKPDqfqkcVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIAFSMKLAG---KNKAERTKRVhEIAKILQL--EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:cd03234 100 ETLTYTAILRLprkSSDAIRKKRV-EDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 170 RVQmraeIASLQRQLGVT--TIYVTHDQ--TEALTMGDRVAVLKGGVL 213
Cdd:cd03234 179 ALN----LVSTLSQLARRnrIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-238 |
2.67e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.61 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-----RDIAMVFQSYALYPHMTVFDN 96
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKlagknkaERTKRVHEIAK---ILQLEP--LLGN---KPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PRK11831 105 VAYPLR-------EHTQLPAPLLHstvMMKLEAvgLRGAaklMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 169 LRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP---VNAFVAGFIGSP 238
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprVRQFLDGIADGP 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-247 |
9.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 9.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGgqDVV--------DLAPKDRDIAMVFQsyalYPH 90
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVvsstskqkEIKPVRKKVGVVFQ----FPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 M-----TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK13643 95 SqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 165 LDAKLRVQMRAEIASLQrQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRpVNAFVAGFIGSPSMNLFE 244
Cdd:PRK13643 175 LDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPKATHFA 252
|
...
gi 1586515037 245 GRL 247
Cdd:PRK13643 253 DQL 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-262 |
1.00e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV------DLAPKDRDIAMVFQsyalYPHM- 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 ----TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK13649 98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 167 AKLRVQMRAEIASLQrQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRpVNAFVAGFIGSPSMNLFEGR 246
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD-VDFLEEKQLGVPKITKFAQR 255
|
250
....*....|....*.
gi 1586515037 247 LASGRIHLPGFSIPLS 262
Cdd:PRK13649 256 LADRGISFSSLPITIE 271
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
1.67e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.11 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD-IAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-219 |
1.94e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGN----SYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGG----------QDVV 69
Cdd:PRK13645 7 IILDNVSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 70 DLApkdRDIAMVFQ--SYALYPHmTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMG 146
Cdd:PRK13645 87 RLR---KEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 147 RAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-227 |
2.48e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYH-AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL--------EEISSGTLSIGGQDVVDLAP 73
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 74 KdrdIAMVFQSyalyPH-----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRA 148
Cdd:PRK13640 85 K---VGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 149 MVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEAlTMGDRVAVLKGGVLQQVDTPKALYHRPV 227
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-236 |
2.88e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEI-----SSGTLSIGGQDV----VDLAPKDRDIAMVFQ 83
Cdd:PRK14243 20 YGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyapdVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHmTVFDNIAFSMKLAG-----KNKAERTKRvhEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGykgdmDELVERSLR--QAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRQLgvTTIYVTHDQTEALTMGDRVAVL---------KGGVLQQVDTPKALYHRPVN- 228
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQq 253
|
250
....*....|.
gi 1586515037 229 ---AFVAGFIG 236
Cdd:PRK14243 254 atrDYVSGRFG 264
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-222 |
2.96e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.13 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-DIAMVFQSYAL 87
Cdd:PRK13536 47 VSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 88 YPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 168 KLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:PRK13536 206 HARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
3.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvDLAPKD-----RD 77
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQS--YALYPhMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLlGNKPAQ-LSGGQRQRVAMGRAMVREPA 154
Cdd:PRK13636 84 VGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
3.84e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.62 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGG----QDVVDLApkdRDIAMVF-QSYALYPHMT 92
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEFA---RRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDniafSMKLAGK----NKAERTKRVHEIAKILQLEPLLgNKPA-QLSGGQRQR--VAMgrAMVREPAAFLMDEPLSNL 165
Cdd:COG4586 113 AID----SFRLLKAiyriPDAEYKKRLDELVELLDLGELL-DTPVrQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQT--EALTmgDRVAVLKGG 211
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEALC--DRVIVIDHG 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-208 |
4.06e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGqdvvdlapkDRDIAMVFQSYALYPHM--TVFDn 96
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLplTVRD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 iAFSMKLAGKNKAERTKRVHEIAKI------LQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:NF040873 77 -LVAMGRWARRGLWRRLTRDDRAAVddalerVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586515037 171 VQMRAEIASLQRQlGVTTIYVTHDQtEALTMGDRVAVL 208
Cdd:NF040873 156 ERIIALLAEEHAR-GATVVVVTHDL-ELVRRADPCVLL 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-211 |
4.48e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV--DLAPKDRDIAMVFQ--SYALYPHMTVF 94
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIAFSMKLAGK-NKAERTKRVHEIAKILQLEPLLGNK-PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:PRK15112 108 QILDFPLRLNTDlEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586515037 173 MRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK15112 188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
5.91e-23 |
|
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: 94.42 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD---IAMV---FQSYALYPHMT 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFsmklagknkaertkrvheiakilqlepllgnkPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDaklrVQ 172
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586515037 173 MRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-212 |
8.73e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 12 TYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSyalyP 89
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 H-----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK13647 89 DdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 165 LDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGV 212
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-226 |
1.36e-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: 99.65 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYG-NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAM 80
Cdd:TIGR03797 452 IEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLagLDVQAVRRQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHmTVFDNIAFSMKLAgknkaerTKRVHEIAKILQLEPLLGNKP-----------AQLSGGQRQRVAMGRAM 149
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARAL 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 150 VREPAAFLMDEPLSNLDAklRVQmRAEIASLQRqLGVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:TIGR03797 604 VRKPRILLFDEATSALDN--RTQ-AIVSESLER-LKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
2.39e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIAM 80
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQSYALYPHMTVFDNIAF----SMKLAGKNK---AERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 154 AAFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-222 |
3.04e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.52 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEiSSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHMTVFDNIAFS 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 101 MKlAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVR-------EPAAFLMDEPLSNLDaklrVQM 173
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD----VAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 174 RAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL------QQVDTPKAL 222
Cdd:COG4138 169 QAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLvasgetAEVMTPENL 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
3.45e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYgNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDL---APKDRD 77
Cdd:PRK10895 1 MATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNIAFSMKLAGK-NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-213 |
3.46e-22 |
|
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: 93.69 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK--DRDIAMVFQSYALYPHmTVFDNI 97
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNK---AERTKRVHEIAKILQLEPL--LGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:cd03248 109 AYGLQSCSFECvkeAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586515037 173 MRaeiASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:cd03248 189 VQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-256 |
3.50e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNS---YHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE----ISSGTLSIGGQDVVDLAP 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 74 KDR------DIAMVFQS--YALYPHMTVFDNIAFSMKL-AGKNKAERTKRVHEIAKILQL---EPLLGNKPAQLSGGQRQ 141
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 142 RVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGvlQQVDTPKA 221
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG--QVVETGKA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1586515037 222 --LYHRPVNAFVAGFIGS-PSMNLFEGRLASgrihLPG 256
Cdd:PRK11022 239 hdIFRAPRHPYTQALLRAlPEFAQDKARLAS----LPG 272
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-219 |
5.88e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.64 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHMTVFDNI 97
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AfsMKLA--GKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAM------VREPAAFLM-DEPLSNLDak 168
Cdd:COG4559 97 A--LGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTSALD-- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 169 LRVQMRaeIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:COG4559 173 LAHQHA--VLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-219 |
1.36e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYAL-YPhMTVFDN 96
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-FTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAfsMKLA-GKNKAERTKRVheIAKILQ---LEPLLGNKPAQLSGGQRQRVAMGRAMVR------EPAAFLMDEPLSNLD 166
Cdd:PRK13548 97 VA--MGRApHGLSRAEDDAL--VAAALAqvdLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 167 akLRVQMRaeIASLQRQL----GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:PRK13548 173 --LAHQHH--VLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-223 |
2.01e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAP--KDRDIA-MVFQSyalyPH 90
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 -----MTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK13633 96 nqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTmGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-211 |
2.06e-21 |
|
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: 90.99 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdrdIAMVFQSyALYPHMTVFDNIA 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 99 FSMKLagknKAERTKRVHEIAkilQLEPLL-----------GNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:cd03250 88 FGKPF----DEERYEKVIKAC---ALEPDLeilpdgdlteiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586515037 168 KLRVQ-MRAEIASLqRQLGVTTIYVTHdQTEALTMGDRVAVLKGG 211
Cdd:cd03250 161 HVGRHiFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-167 |
2.24e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNsyHAI-KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIggqdvvdlaPKDRDIAMVFQS 84
Cdd:COG0488 1 LENLSKSFGG--RPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 YALYPHMTVFDNIAFSMKLAGKNKAERTK--------------------------------RVHEIAKILQLEPLLGNKP 132
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586515037 133 -AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-222 |
3.33e-21 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 91.32 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 26 TIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIggqDVVDLAPKDRDIAMVFQsyalyphMTVFDNIAFSMKLAG 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYE-------GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 106 KNKAERTkrvhEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLG 185
Cdd:cd03237 91 THPYFKT----EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586515037 186 VTTIYVTHDQTEALTMGDRVAVLKG--GVLQQVDTPKAL 222
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFEGepSVNGVANPPQSL 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-194 |
4.97e-21 |
|
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: 90.57 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTL---SIGGQ-DVVDLAPKD------RDIAMVFQSYALY 88
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWvDLAQASPREilalrrRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 89 PHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180
....*....|....*....|....*..
gi 1586515037 168 KLRVQMRAEIASLQRQlGVTTIYVTHD 194
Cdd:COG4778 186 ANRAVVVELIEEAKAR-GTAIIGIFHD 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-223 |
5.06e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSyalyPH- 90
Cdd:PRK13648 19 SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 ----MTVFDNIAFSMKlagkNKAERTKRVHEI-AKILQLEPLLG---NKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:PRK13648 95 qfvgSIVKYDVAFGLE----NHAVPYDEMHRRvSEALKQVDMLEradYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTmGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-213 |
5.46e-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: 90.30 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 25 LTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlAPKDRDIAMVFQSYAL---YP---HMTVFDNIA 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASP---GKGWRHIGYVPQRHEFawdFPisvAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 99 FSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIA 178
Cdd:TIGR03771 78 GHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1586515037 179 SLQrQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:TIGR03771 158 ELA-GAGTAILMTTHDLAQAMATCDRVVLLNGRVI 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-213 |
6.28e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 94.40 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHm 91
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFS-MKLAGKNKAERTKRVHEIAKILQLEPL-----LGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:TIGR02203 421 TIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLgldtpIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 166 DAKLRVQMRAEIASLQRqlGVTTIYVTHDQTeALTMGDRVAVLKGGVL 213
Cdd:TIGR02203 501 DNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-211 |
7.69e-21 |
|
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: 90.24 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMVFQSYALYpHM 91
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSmklagkNKAERTKRVHEIAK-------ILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:cd03252 91 SIRDNIALA------DPGMSMERVIEAAKlagahdfISELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 161 PLSNLDAKlrvQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:cd03252 165 ATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-230 |
7.89e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKS-TALRMIAGLE----EISSGTLSIGGQDVVDlAPKDR-------DIAMV 81
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvVYPSGDIRFHGESLLH-ASEQTlrgvrgnKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQS--YALYPHMTVFDNIA--FSMKLAGKNKAERTKRVH--EIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:PRK15134 98 FQEpmVSLNPLHTLEKQLYevLSLHRGMRREAARGEILNclDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAF 230
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-234 |
8.03e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSyhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV-VDLAPKDRDIAMVFQS 84
Cdd:TIGR01257 934 LVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 YALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 165 LDAKLRVQMRAEIasLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYhrpvNAFVAGF 234
Cdd:TIGR01257 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLK----NCFGTGF 1155
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-193 |
8.67e-21 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 94.24 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLaPKDR---DIAMVFQSYALYpHMTVFDN 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAF---SMKLAGKNKAERTKRVHEI--AKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRV 171
Cdd:TIGR03796 573 LTLwdpTIPDADLVRACKDAAIHDVitSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
170 180
....*....|....*....|..
gi 1586515037 172 QMRAEIaslqRQLGVTTIYVTH 193
Cdd:TIGR03796 653 IIDDNL----RRRGCTCIIVAH 670
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
9.08e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVV--DLAPKDRDI 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 AMVFQS---YALYPhmTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAA 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 156 FLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-215 |
1.04e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLeeIS-SGTLSIGGQDVVDLAPKD--RDIAMVFQSYALyPHMTVFDNIAF 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMKLAGKnkaERTKRVHEIAKILQLEPLL--------GNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK--L 169
Cdd:PRK11174 446 GNPDASD---EQLQQALENAWVSEFLPLLpqgldtpiGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHseQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586515037 170 RVqMRAEIASLQRQlgvTTIYVTHdQTEALTMGDRVAVLKGGVLQQ 215
Cdd:PRK11174 523 LV-MQALNAASRRQ---TTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-211 |
1.31e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYgNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL---EEISSGTLSIGGQDVVDLAPKDRDI- 78
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 ------AMVFQSYALYPHMTVFDNIAFSMklAGKNKAERT----------KRVHEIAKILQLEPLLGNKPAQLSGGQRQR 142
Cdd:PRK09984 83 ksrantGYIFQQFNLVNRLSVLENVLIGA--LGSTPFWRTcfswftreqkQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 143 VAMGRAMVREPAAFLMDEPLSNLDAK-LRVQMRAeIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-207 |
1.33e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 21 KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRdIAMVFQSYALYPHMTVFDNIAFS 100
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 101 MKLAGknkaERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlRVQMRAEIASL 180
Cdd:PRK13539 98 AAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRA 172
|
170 180 190
....*....|....*....|....*....|..
gi 1586515037 181 QRQLGVTTIYVTH-----DQTEALTMGDRVAV 207
Cdd:PRK13539 173 HLAQGGIVIAATHiplglPGARELDLGPFAAE 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-226 |
8.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLA--PKDRDI-A 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQS-YALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDqTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-222 |
8.87e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 7 DKICKTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ- 83
Cdd:PRK10253 11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 -------------SYALYPHMTVFDniafsmklagKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMV 150
Cdd:PRK10253 90 attpgditvqelvARGRYPHQPLFT----------RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 151 REPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
9.63e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIggqdvvdlaPKDRDIAMVFQ-SY--------AL-YP 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HmtvfDNIAFSMKlagknkaertkrvhEIAKILQ---LEPLLG------NKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:COG4178 450 A----TAEAFSDA--------------ELREALEavgLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 1586515037 161 PLSNLDAKLRVQMraeIASLQRQL-GVTTIYVTH 193
Cdd:COG4178 512 ATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-222 |
1.15e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEiSSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHMTVFDNIAFS 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 101 MKlAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRvamgramVREPAAFL--------------MDEPLSNLD 166
Cdd:PRK03695 94 QP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQR-------VRLAAVVLqvwpdinpagqlllLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 167 AKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL------QQVDTPKAL 222
Cdd:PRK03695 166 VAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLlasgrrDEVLTPENL 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-256 |
1.22e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.63 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL---EEISSGTLSIGGQDVVDLAPKD------RDIAMVFQS--YAL 87
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 88 YPHMTVFDNIAFSMKL-AGKNKA---ERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLhKGMSKAeafEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 164 NLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGFIGS-PSMNL 242
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAvPRLDA 270
|
250
....*....|....
gi 1586515037 243 FEGRLASgrihLPG 256
Cdd:PRK09473 271 EGESLLT----IPG 280
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-213 |
2.04e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 90.19 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMVFQSYALYPHmTVFDNI 97
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiADPAWLRRQMGVVLQENVLFSR-SIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSmklagkNKAERTKRVHEIAK-------ILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:TIGR01846 552 ALC------NPGAPFEHVIHAAKlagahdfISELpqgyNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 167 AKLRvqmraeiASLQRQL-----GVTTIYVTHdQTEALTMGDRVAVLKGGVL 213
Cdd:TIGR01846 626 YESE-------ALIMRNMreicrGRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-211 |
2.22e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD-IAMVFQSyalyPHmt 92
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQR----PY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIafsmklagknkaertkrvheiakilqlepLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:cd03247 86 LFDTT-----------------------------LRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586515037 173 MRAEIASLQRqlGVTTIYVTHDQTeALTMGDRVAVLKGG 211
Cdd:cd03247 137 LLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENG 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-223 |
3.31e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 12 TYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQ----DVVDLAPKDRDIAMVFQS--- 84
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVGIVFQNpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 --YAlyPhmTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:PRK13639 90 qlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALY 223
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-219 |
3.52e-19 |
|
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: 89.09 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE--------------------------------ISSGTLSIGGQ 66
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverpskvgepcpVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 67 DVVDLAPKD-----RDIAMVFQ-SYALYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQR 140
Cdd:TIGR03269 95 DFWNLSDKLrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 141 QRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHdQTEALT-MGDRVAVLKGGVLQQVDTP 219
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDKAIWLENGEIKEEGTP 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-213 |
3.87e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAP---KDRDIAMVFQSY 85
Cdd:PRK15439 17 ISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMklagKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK15439 96 LLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 166 DAKLRVQMRAEIASLQrQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:PRK15439 172 TPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-193 |
1.06e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.71 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMV 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrtVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYpHMTVFDNIafsmkLAGKNKAERTKrVHEIAKILQ-----------LEPLLGNKPAQLSGGQRQRVAMGRAMV 150
Cdd:PRK13657 415 FQDAGLF-NRSIEDNI-----RVGRPDATDEE-MRAAAERAQahdfierkpdgYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586515037 151 REPAAFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTH 193
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
1.43e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 1 MAVVVLDKICKTYgNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD---RD 77
Cdd:PRK11288 2 SPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 78 IAMVFQSYALYPHMTVFDNI---AFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGGvlQQVDT 218
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG--RYVAT 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-215 |
1.53e-18 |
|
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: 87.49 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLapkDRDIAMVFQ 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SY-ALYPHM---TVFDNIAFSMKlaGKNKAERTKRVHEIAKI--------LQLEPLLGNKPAQLSGGQRQRVAMGRAMVR 151
Cdd:TIGR01193 551 NYlPQEPYIfsgSILENLLLGAK--ENVSQDEIWAACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 152 EPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQlgvTTIYVTHDQTEAlTMGDRVAVL-KGGVLQQ 215
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLdHGKIIEQ 689
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-236 |
1.57e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 35 LVGPSGCGKSTALRMIAGL-EEIS----SGTLSIGGQDVV---DLAPKDRDIAMVFQSYALYPhMTVFDNIAFSM---KL 103
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFnyrDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVrahKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 104 AGKN--KAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQ 181
Cdd:PRK14271 131 VPRKefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 182 RQLgvTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNA----FVAGFIG 236
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-222 |
1.59e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.49 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGE---FLilvGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlAPKDRDIAM----VFQSYALYPHM 91
Cdd:NF033858 281 AVDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATRRrvgyMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRV 171
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 172 QMRAEIASLQRQLGVtTIYV-THDQTEALTMgDRVAVLKGG-VLqQVDTPKAL 222
Cdd:NF033858 435 MFWRLLIELSREDGV-TIFIsTHFMNEAERC-DRISLMHAGrVL-ASDTPAAL 484
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-194 |
1.63e-18 |
|
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: 87.03 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-RDIAMVFQSYALYPHM 91
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSMKLAGKNKAERTKRVHEIAKILQ-----LEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALERVGLADWLRalpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 1586515037 167 AKLRVQMRAEIASLQRqlGVTTIYVTHD 194
Cdd:TIGR02868 504 AETADELLEDLLAALS--GRTVVLITHH 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-194 |
1.87e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvVDLA--PKDRDiam 80
Cdd:COG0488 315 VLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--VKIGyfDQHQE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 vfqsyALYPHMTVFDNIAfsmklagknkaertkRVHEIAKILQLEPLLG---------NKP-AQLSGGQRQRVAMGRAMV 150
Cdd:COG0488 389 -----ELDPDKTVLDELR---------------DGAPGGTEQEVRGYLGrflfsgddaFKPvGVLSGGEKARLALAKLLL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586515037 151 REPAAFLMDEPLSNLDaklrVQMRAEIASLQRQLGVTTIYVTHD 194
Cdd:COG0488 449 SPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHD 488
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-213 |
2.06e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV------------VDLAPKDRdiamvfQSY 85
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairagIAYVPEDR------KGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSM--KLAGK---NKAERTKRVHEIAKILQLEPLLGNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:COG1129 340 GLVLDLSIRENITLASldRLSRGgllDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 160 EPLSNLD--AKlrvqmrAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:COG1129 420 EPTRGIDvgAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
2.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTL----------------SIGGQDVVDLAPKDRDI---- 78
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekEKVLEKLVIQKTRFKKIkkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 79 ------AMVFQ--SYALYpHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:PRK13651 102 eirrrvGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-227 |
2.89e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK--DRDIAMVFQSYALYPHMTVFDNIAFS 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 101 M----KLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAE 176
Cdd:PRK10575 110 RypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 177 IASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPV 227
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-287 |
4.92e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYAL------------ 87
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefdvrqvvem 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 88 --YPHMTVFDniafSMKLAGKNKAERTKRVHEIAKilqleplLGNKP-AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK09536 101 grTPHRSRFD----TWTETDRAAVERAMERTGVAQ-------FADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 165 LDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPV--NAFVAGFI------- 235
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTlrAAFDARTAvgtdpat 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 236 GSPSMNLFEGR----LASG-RIHLPGfsiplSGGALERAPGLSAFEGKDVIFGVRPE 287
Cdd:PRK09536 249 GAPTVTPLPDPdrteAAADtRVHVVG-----GGQPAARAVSRLVAAGASVSVGPVPE 300
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-193 |
9.31e-18 |
|
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: 80.87 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK-DRDIAMVFQSYALYPHMTVFDNIAFSM 101
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 102 KLAGKnkAERTkrvheIAKILQLEPLLG--NKPA-QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD----AKLRVQMR 174
Cdd:TIGR01189 99 AIHGG--AQRT-----IEDALAAVGLTGfeDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvALLAGLLR 171
|
170
....*....|....*....
gi 1586515037 175 AEIASlqrqlGVTTIYVTH 193
Cdd:TIGR01189 172 AHLAR-----GGIVLLTTH 185
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-223 |
1.11e-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: 81.80 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTL-----SIGGQDVVDLAPKDR------DIA 79
Cdd:TIGR02323 11 KSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrSGAELELYQLSEAERrrlmrtEWG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVFdniafsmklAGKNKAERTKRV------------HEIAKILQLEP-LLGNKPAQLSGGQRQRVAMG 146
Cdd:TIGR02323 90 FVHQNPRDGLRMRVS---------AGANIGERLMAIgarhygnirataQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 147 RAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVL-------QQVDTP 219
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltdQVLDDP 240
|
....
gi 1586515037 220 KALY 223
Cdd:TIGR02323 241 QHPY 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-193 |
1.41e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.10 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 16 SYHA----IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYp 89
Cdd:COG5265 366 GYDPerpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVFDNIAFsmklaGKNKAERTKrVHEIAKILQLEPLLGNKPAQ-----------LSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:COG5265 445 NDTIAYNIAY-----GRPDASEEE-VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTH 193
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-216 |
1.64e-17 |
|
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: 80.00 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS---SGTLSIGGQDVVDLAPK-DRDIAMVFQSYALYPHMTVFD 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKLAGknkaertkrvHEIAKilqlepllgnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRA 175
Cdd:cd03233 103 TLDFALRCKG----------NEFVR-------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586515037 176 EIASLQRQLGVTTIyVTHDQT--EALTMGDRVAVLKGGvlQQV 216
Cdd:cd03233 160 CIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEG--RQI 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-213 |
2.02e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 2 AVVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDvVDLAPKDRDIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYAL---YPhMTVFDNIAFS----MKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:PRK15056 84 PQSEEVdwsFP-VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 155 AFLMDEPLSNLDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:PRK15056 163 VILLDEPFTGVD----VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-226 |
2.45e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLApkDRDIA---MV--FQSYALYPHMTV 93
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP--GHQIArmgVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 94 FDN-------------IAFSMKLAGKNKAERTK--RVHEIAKILQLEPLlGNKPA-QLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK11300 98 IENllvaqhqqlktglFSGLLKTPAFRRAESEAldRAATWLERVGLLEH-ANRQAgNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQteALTMG--DRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDM--KLVMGisDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-225 |
2.59e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdVVDLAPKD-----RDIAMVFQSyalyPHMTVF 94
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGllalrQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 -----DNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFR-HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 169 LRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHR 225
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-196 |
2.94e-17 |
|
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: 78.35 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIggqdvvdlaPKDRDIAMVFQ-SY---------ALYP 89
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPYlplgtlreqLIYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 HMTVfdniafsmklagknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDakl 169
Cdd:cd03223 88 WDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180
....*....|....*....|....*..
gi 1586515037 170 rVQMRAEIASLQRQLGVTTIYVTHDQT 196
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVGHRPS 149
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-211 |
3.02e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNsYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQD--VVDLA----PKDR-----DIA 79
Cdd:PRK11701 14 KLYGP-RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqLRDLYalseAERRrllrtEWG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYALYPHMTVfdniafsmkLAGKNKAER-------------------TKRVhEIAkilqlEPLLGNKPAQLSGGQR 140
Cdd:PRK11701 93 FVHQHPRDGLRMQV---------SAGGNIGERlmavgarhygdiratagdwLERV-EID-----AARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 141 QRVAMGRAMVREPAAFLMDEPLSNLDakLRVQMRA--EIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-219 |
3.18e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 15 NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIG----GQDVVDLAPKD--------------R 76
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkelrR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 77 DIAMVFQ--SYALYPHmTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQL-EPLLGNKPAQLSGGQRQRVAMGRAMVREP 153
Cdd:PRK13631 117 RVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 154 AAFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-211 |
6.93e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTY-GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD-RD-IAMVF 82
Cdd:PRK11160 341 LNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHmTVFDNIAFSMKLAGKNK-AERTKRVhEIAKILQ-LEPL---LGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK11160 421 QRVHLFSA-TLRDNLLLAAPNASDEAlIEVLQQV-GLEKLLEdDKGLnawLGEGGRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 158 MDEPLSNLDAklrvQMRAEIASLQRQL--GVTTIYVTHDQTeALTMGDRVAVLKGG 211
Cdd:PRK11160 499 LDEPTEGLDA----ETERQILELLAEHaqNKTVLMITHRLT-GLEQFDRICVMDNG 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-182 |
1.07e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVD--LAPKDRDIAMVFQSYALYpHMTVFDN 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFsmklAGKNKAER------TKRVHEIAKILQLE----PLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK11176 437 IAY----ARTEQYSReqieeaARMAYAMDFINKMDngldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170
....*....|....*.
gi 1586515037 167 AKLRVQMRAEIASLQR 182
Cdd:PRK11176 513 TESERAIQAALDELQK 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-168 |
2.08e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlaPKDRDiamVFQSYALY--------PHMTV 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRD---EYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 94 FDNIAFSMKLAGKNKAERtkrvheIAKILQLEPLLG--NKPA-QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEA------LWEALAQVGLAGfeDVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-195 |
2.67e-16 |
|
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: 75.18 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLsiggqdvvdlapkdrdiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 syalyphmtvfdniafsmklagknkaertkRVHEIAKILQLEpllgnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:cd03221 58 ------------------------------TWGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 1586515037 164 NLDAKLRVQMRAEIASLQRqlgvTTIYVTHDQ 195
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
2.97e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKS----TALRMI-AGLEEiSSGTLSIGGQDVVDLAPKDRDIAMVFQS--YALYPHMT 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKR-------VHEIAKILQLEPLlgnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:PRK10418 98 MHTHARETCLALGKPADDATLTaaleavgLENAARVLKLYPF------EMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 166 DAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-219 |
3.04e-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: 76.76 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKST---AL-RMIagleEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHmT 92
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllALfRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFsmkLAGKNKAER---TKRVHEIAKILQLEPLLGNK----PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:cd03244 94 IRSNLDP---FGEYSDEELwqaLERVGLKEFVESLPGGLDTVveegGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 166 D----AKLRVQMRAEIAslqrqlGVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:cd03244 171 DpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-194 |
1.09e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 78.29 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 26 TIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGgqdvVDLAPK------DRDiamvfqsyalyphMTVFDNIAF 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYKpqyispDYD-------------GTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 smklAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIAS 179
Cdd:COG1245 425 ----ANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170
....*....|....*
gi 1586515037 180 LQRQLGVTTIYVTHD 194
Cdd:COG1245 501 FAENRGKTAMVVDHD 515
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-258 |
1.28e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 30 GEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVFQSYALYPHMTVFDNIAFSMKLAGKN-- 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKsl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 108 -KAERTKRVHEIAKILQL----EPLLGNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQ 181
Cdd:PLN03211 174 tKQEKILVAESVISELGLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 182 rQLGVTTIYVTHD-QTEALTMGDRVAVLKGGvlqqvdtpKALY----HRPVNAF-VAGFIGSPSMNL--FEGRLASGRIH 253
Cdd:PLN03211 254 -QKGKTIVTSMHQpSSRVYQMFDSVLVLSEG--------RCLFfgkgSDAMAYFeSVGFSPSFPMNPadFLLDLANGVCQ 324
|
....*
gi 1586515037 254 LPGFS 258
Cdd:PLN03211 325 TDGVS 329
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-210 |
1.47e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.93 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 8 KICKTYGnsyhaikDLSL-----TIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGgqdvVDLAPKDRDIAMVF 82
Cdd:PRK13409 345 DLTKKLG-------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPQYIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 qsyalypHMTVFDNIAFSMKLAGKNKAErtkrvHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPL 162
Cdd:PRK13409 414 -------DGTVEDLLRSITDDLGSSYYK-----SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586515037 163 SNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKG 210
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-211 |
1.73e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISS--GTLSIGGQDVVDLAPKDRD---IAMVFQ 83
Cdd:TIGR02633 7 IVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTEragIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKLAGK----NKAERTKRVHEIAKILQLEPLLGNKP-AQLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPggrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 159 DEPLSNLDAKlRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:TIGR02633 166 DEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-161 |
2.44e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR---DIA 79
Cdd:NF033858 1 VARLEGVSHRYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQSYA--LYPHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLgNKPA-QLSGGQRQRVAMGRAMVREPAAF 156
Cdd:NF033858 80 YMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFA-DRPAgKLSGGMKQKLGLCCALIHDPDLL 158
|
....*
gi 1586515037 157 LMDEP 161
Cdd:NF033858 159 ILDEP 163
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-211 |
2.54e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLE--EISSGTLSIGGQDVVDLAPKDR---DIAMVFQSYALYPHMTVF 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DniaFsMKLAGKNKAERT-------KRVHEIAKILQLEPLLGNKP--AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL 165
Cdd:COG0396 96 N---F-LRTALNARRGEElsareflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 166 DA-KLRVqMRAEIASLQRQlGVTTIYVTH-----DQTEAltmgDRVAVLKGG 211
Cdd:COG0396 172 DIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIKP----DFVHVLVDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-216 |
3.55e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD---RDIAMVFQSY---ALYPHMTV 93
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 94 FDNIAFS--MKLAGK-------NKAERTKRVHEIAKILQLE-PLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK09700 359 AQNMAISrsLKDGGYkgamglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 164 NLDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQQV 216
Cdd:PRK09700 439 GID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-226 |
4.47e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.33 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE----ISSGTLSIGGQDVVDLAPKDR------DIAMVFQ--SY 85
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSM---KLAGK---NKAERTKRVHEIAK---ILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:COG4170 101 CLDPSAKIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHrvgIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRP 226
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-235 |
4.49e-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: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 29 DGEFLILVGPSGCGKSTALRMIAGLEEISSGTLsiggqdvvDLAPKDRDIAMVFQSYALYPHMT--VFDNIAFSMK---- 102
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKpqyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 103 ------LAGK-----NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRV 171
Cdd:cd03236 97 dlipkaVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 172 QMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKG--GVLQQVDTPKALyHRPVNAFVAGFI 235
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGepGAYGVVTLPKSV-REGINEFLDGYL 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-211 |
5.15e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLsiggqdvvdLApkDRDIAMVFQSyALYPHMTVFDNIAF 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WA--ERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SmklagknKAERTKRVHEIAKILQLEPLL-----------GNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PTZ00243 744 F-------DEEDAARLADAVRVSQLEADLaqlgggleteiGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586515037 169 LRVQMRAEIAsLQRQLGVTTIYVTHdQTEALTMGDRVAVLKGG 211
Cdd:PTZ00243 817 VGERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDG 857
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-215 |
8.04e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.90 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHm 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSMKLAGKNKAERTKR---VHEiaKILQL----EPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK10789 404 TVANNIALGRPDATQQEIEHVARlasVHD--DILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 165 LDAklrvQMRAEIASLQRQLGVT-TIYVTHDQTEALTMGDRVAVLK-GGVLQQ 215
Cdd:PRK10789 482 VDG----RTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQhGHIAQR 530
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-217 |
2.80e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 6 LDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQ 83
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMtvfdniafsmkLAGKNKAERTKRVHEIAKILQLE---PLLGNKPA--QLSGGQRQRVAMGRAMVREPAAFLM 158
Cdd:PRK10522 405 DFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 159 DEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQtEALTMGDRVAVLKGGVLQQVD 217
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSELT 531
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-203 |
3.74e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV-VDLAPKDRDIAMVFQSYALYPHMTVFDNIA 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 99 FSMKLAGKNKAertkrVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIA 178
Cdd:PRK13540 97 YDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170 180
....*....|....*....|....*
gi 1586515037 179 SLQRQLGvtTIYVTHDQTEALTMGD 203
Cdd:PRK13540 172 EHRAKGG--AVLLTSHQDLPLNKAD 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-194 |
4.67e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTlsiggqdvVDLAPKDRdIAMVF 82
Cdd:PRK09544 4 LVSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR-IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHM--TVfdnIAFSMKLAGKNKAE---RTKRVHEiAKILQlepllgnKPAQ-LSGGQRQRVAMGRAMVREPAAF 156
Cdd:PRK09544 74 QKLYLDTTLplTV---NRFLRLRPGTKKEDilpALKRVQA-GHLID-------APMQkLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586515037 157 LMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHD 194
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-211 |
1.17e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 69.67 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 12 TYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD------IAMVFQSY 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYpHMTVFDNIAFSMKLagkNKaERTKRVHEIAKI---LQLEPL-----LGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:cd03290 89 WLL-NATVEENITFGSPF---NK-QRYKAVTDACSLqpdIDLLPFgdqteIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 158 MDEPLSNLDAKLRVQ-MRAEIASLQRQLGVTTIYVTHdQTEALTMGDRVAVLKGG 211
Cdd:cd03290 164 LDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-193 |
1.51e-13 |
|
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: 72.09 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIggqdvvdlaPKDRDIAMVFQSyalyPHMTV---FDN 96
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLgtlRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSM-KLAGKNKAERTKRVHEIAKILQLEPLL----GNKPAQ-----LSGGQRQRVAMGRAMVREPAAFLMDEPLSnld 166
Cdd:TIGR00954 535 IIYPDsSEDMKRRGLSDKDLEQILDNVQLTHILeregGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTS--- 611
|
170 180
....*....|....*....|....*..
gi 1586515037 167 aKLRVQMRAEIASLQRQLGVTTIYVTH 193
Cdd:TIGR00954 612 -AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-211 |
1.60e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRDIAMVF------QSYALYPHMT 92
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIA---FSMKLAGKNKAERTKRVHEIAK--ILQLE---PLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:COG3845 353 VAENLIlgrYRRPPFSRGGFLDRKAIRAFAEelIEEFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRG 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586515037 165 LDAKLRVQMRAEIASLqRQLGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:COG3845 433 LDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-195 |
1.73e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTlsigGQDVVDLAPKDRDIAMVfqsYALYPHMTVFDNI 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----GCVDVPDNQFGREASLI---DAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFsMKLAGKNKAertkrvheiakilqlePLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEI 177
Cdd:COG2401 117 EL-LNAVGLSDA----------------VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*...
gi 1586515037 178 ASLQRQLGVTTIYVTHDQ 195
Cdd:COG2401 180 QKLARRAGITLVVATHHY 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-225 |
1.83e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 72.29 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdrdIAMVFQSyALYPHMTVFDNIAFSMK 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 103 LAGKnkaeRTKRVHEIAKIL-QLEPL-------LGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMR 174
Cdd:TIGR00957 725 LNEK----YYQQVLEACALLpDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 175 AEIASLQRQL-GVTTIYVTHDQTeALTMGDRVAVLKGGVLQQVDTPKALYHR 225
Cdd:TIGR00957 801 EHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-166 |
2.23e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGgqDVVDLAPKD--RDiam 80
Cdd:TIGR03719 322 VIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDqsRD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 vfqsyALYPHMTVFDNIAFS---MKLAGKNKAERT-------------KRVheiakilqlepllgnkpAQLSGGQRQRVA 144
Cdd:TIGR03719 396 -----ALDPNKTVWEEISGGldiIKLGKREIPSRAyvgrfnfkgsdqqKKV-----------------GQLSGGERNRVH 453
|
170 180
....*....|....*....|...
gi 1586515037 145 MGRaMVREPA-AFLMDEPLSNLD 166
Cdd:TIGR03719 454 LAK-TLKSGGnVLLLDEPTNDLD 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-243 |
3.23e-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: 71.58 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTY-GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlapkdrDIAMV 81
Cdd:TIGR01257 1937 ILRLNELTKVYsGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIA-------FSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPA 154
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLtgrehlyLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 155 AFLMDEPLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAFVAGF 234
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM 2169
|
250
....*....|
gi 1586515037 235 -IGSPSMNLF 243
Cdd:TIGR01257 2170 kIKSPKDDLL 2179
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
3.53e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGtlsiggqdVVDLAPkDRDIAMVF 82
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------EARPQP-GIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 QSYALYPHMTVFDNI---------------AFSMKLAGKNkAERTKRVHEIAKI-------------LQLE--------P 126
Cdd:TIGR03719 75 QEPQLDPTKTVRENVeegvaeikdaldrfnEISAKYAEPD-ADFDKLAAEQAELqeiidaadawdldSQLEiamdalrcP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 127 LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlrvqmraEIASLQRQL----GvTTIYVTHD 194
Cdd:TIGR03719 154 PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLqeypG-TVVAVTHD 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-211 |
7.08e-13 |
|
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: 66.78 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLE--EISSGTLSIGGQDVVDLAPKDR---DIAMVFQSYALYPHMTVF 94
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DniafsmklagknkaertkrvheiakilqlepLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlRVQMR 174
Cdd:cd03217 96 D-------------------------------FLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586515037 175 AEIASLQRQLGVTTIYVTHDQTEALTM-GDRVAVLKGG 211
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDG 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-193 |
7.12e-13 |
|
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: 66.75 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK-DRDIAMVFQSYALYPHMTVFDNIAFSM 101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 102 KLAGknkaerTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD----AKLRVQMRAEI 177
Cdd:cd03231 99 ADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAGHC 172
|
170
....*....|....*.
gi 1586515037 178 ASlqrqlGVTTIYVTH 193
Cdd:cd03231 173 AR-----GGMVVLTTH 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-215 |
8.10e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSiggqdvvdlapKDRDIAMVFQSYALY 88
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 89 PHMTVFDNIAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586515037 169 LRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQ 215
Cdd:PRK13546 178 FAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-208 |
8.87e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 57 SSGTLSIGGQDVVDLAPKD-RDIAMVFQSYALYPHMTVFDNIAFsmklaGKNKAER--TKRVHEIAKILQLEPLLGNK-- 131
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKF-----GKEDATRedVKRACKFAAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 132 ------PAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHdQTEALTMGDRV 205
Cdd:PTZ00265 1350 tnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428
|
...
gi 1586515037 206 AVL 208
Cdd:PTZ00265 1429 VVF 1431
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-213 |
1.18e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 24 SLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV------------VDLAPKDRdiamvfQSYALYPHM 91
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdairagIMLCPEDR------KAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 TVFDNIAFSMK----LAG---KNKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK11288 347 SVADNINISARrhhlRAGcliNNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 165 LDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:PRK11288 427 ID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-210 |
2.06e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlAPKDRDIAMVFQSYALYPHMTVFDNIAFSMK 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 103 LAGKnkaeRTKRVHEIAkiLQLEPLLGNKPA---QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlRVQMRAEIAS 179
Cdd:PRK13543 109 LHGR----RAKQMPGSA--LAIVGLAGYEDTlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMIS 181
|
170 180 190
....*....|....*....|....*....|.
gi 1586515037 180 LQRQLGVTTIYVTHDQTEALTMGDRVAVLKG 210
Cdd:PRK13543 182 AHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-193 |
2.07e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 21 KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIG-GQDVVDLAPK--DRDIAMVFQSYALYPHmTVFDNI 97
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSM-------------------KLAGKNKAER---------------------------------------TKRV--HE 117
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedgndSQENKNKRNScrakcagdlndmsnttdsneliemrknyqtikdsevvdvSKKVliHD 560
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 118 IAKIL--QLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTH 193
Cdd:PTZ00265 561 FVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-211 |
5.77e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLeeiSSGTLSIGGQDVVDLAPKDRDI-----AMVFQSYALYPHMT 92
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDAKEmraisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERTKRVHEIAKILQLeplLGNKPAQ------------LSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQA---LGLRKCAntrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 161 PLSNLD---AKLRVQMRAEIAslqrQLGVTTIYVTHDQT-EALTMGDRVAVLKGG 211
Cdd:TIGR00955 193 PTSGLDsfmAYSVVQVLKGLA----QKGKTIICTIHQPSsELFELFDKIILMAEG 243
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-170 |
8.89e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.74 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 22 DLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVvdlapkdRDIAMVFQSY-----ALYPHMTVFDN 96
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-------NNIAKPYCTYighnlGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 97 IAFSMKLAgkNKAErtkRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:PRK13541 91 LKFWSEIY--NSAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-212 |
2.17e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.70 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdrdIAMVFQSYALYPHmTVFDNIAF 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMklagknkAERTKRVHEIAKILQLEP-----------LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDak 168
Cdd:TIGR01271 510 GL-------SYDEYRYTSVIKACQLEEdialfpekdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD-- 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586515037 169 lrVQMRAEI--ASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGV 212
Cdd:TIGR01271 581 --VVTEKEIfeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-211 |
2.52e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.72 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdrdIAMVFQSYALYPHmTVFDNIAF 99
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 100 SMklagknkAERTKRVHEIAKILQLEP-----------LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAK 168
Cdd:cd03291 121 GV-------SYDEYRYKSVVKACQLEEditkfpekdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586515037 169 LRVQMrAEIASLQRQLGVTTIYVThDQTEALTMGDRVAVLKGG 211
Cdd:cd03291 194 TEKEI-FESCVCKLMANKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-215 |
3.08e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK--DRDIAMVFQSYALYPH 90
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 mTVFDNIAFsmklaGKNKAErtKRVHEIAKILQLEPL-----------LGNKPAQLSGGQRQRVAMGRAMVREPAAFLMD 159
Cdd:PRK10790 430 -TFLANVTL-----GRDISE--EQVWQALETVQLAELarslpdglytpLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 160 EPLSNLDAKLRVQMRAEIASLQRQlgvTTIYVTHDQTEALTMGDRVAVL-KGGVLQQ 215
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLhRGQAVEQ 555
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-211 |
3.70e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 9 ICKTYGnSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISS--GTLSIGGQDVVDLAPKDRD---IAMVFQ 83
Cdd:PRK13549 11 ITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTEragIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 84 SYALYPHMTVFDNIAFSMKL--AGK-NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDE 160
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEItpGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 161 PLSNLDAKLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-219 |
6.24e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.27 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDV--VDLAPKDRDIAMVFQsyalyphmtvfDN 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstIPLEDLRSSLTIIPQ-----------DP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDaklrVQMRAE 176
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586515037 177 IASLQRQL--GVTTIYVTHdQTEALTMGDRVAVLKGGVLQQVDTP 219
Cdd:cd03369 164 IQKTIREEftNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-211 |
8.06e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-DIAMVFQSY-----ALYPHMTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 94 FDNIA------FSmKLAG--KNKAERTKRVHEIA----KILQLEPLLGNkpaqLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:PRK10762 348 KENMSltalryFS-RAGGslKHADEQQAVSDFIRlfniKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 162 LSNLDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK10762 423 TRGVD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-218 |
8.78e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 18 HAIKDLSLTIHDGEFLILVGPSGCGKSTALR-MIAGLEEISSGTLSIGGQdvVDLAPKdrdIAMVFQSyalyphmTVFDN 96
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT--VAYVPQ---VSWIFNA-------TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 97 IAFSMKLAgKNKAERTKRVHEIAKILQLEP-----LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRV 171
Cdd:PLN03130 699 ILFGSPFD-PERYERAIDVTALQHDLDLLPggdltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586515037 172 QMRAEiaSLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDT 218
Cdd:PLN03130 778 QVFDK--CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-289 |
9.60e-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: 56.82 E-value: 9.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 236 GSPSMNLFEGRLASGRIHLP--GFSIPLSGGaleRAPGLSAFEGKDVIFGVRPEDL 289
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLggGVTLPLPEG---QVLALKLYVGKEVILGIRPEHI 53
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-166 |
1.34e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 16 SYHAIKDLS-LTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMvfqsyalyphmT 92
Cdd:PRK11147 14 SDAPLLDNAeLHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVEG-----------T 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAfsmklAG-KNKAERTKRVHEIAKILQLEP--------------------------------LLGNKP----AQL 135
Cdd:PRK11147 83 VYDFVA-----EGiEEQAEYLKRYHDISHLVETDPseknlnelaklqeqldhhnlwqlenrinevlaQLGLDPdaalSSL 157
|
170 180 190
....*....|....*....|....*....|.
gi 1586515037 136 SGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-213 |
1.77e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 21 KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDR-DIAMVF-----QSYALYPHMTVF 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIA------FSMKLAGKNKAERTKRVHEIAKILQLEPllgNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDA 167
Cdd:PRK15439 360 WNVCalthnrRGFWIKPARENAVLERYRRALNIKFNHA---EQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586515037 168 KLRVQMRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGGVL 213
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-166 |
1.85e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 3 VVVLDKICKTYGNSYhAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGgqDVVDLAPKD--RDiam 80
Cdd:PRK11819 324 VIEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKLAYVDqsRD--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 vfqsyALYPHMTVFDNIafS-----MKLAGKNKAERT-------------KRVheiakilqlepllgnkpAQLSGGQRQR 142
Cdd:PRK11819 398 -----ALDPNKTVWEEI--SggldiIKVGNREIPSRAyvgrfnfkggdqqKKV-----------------GVLSGGERNR 453
|
170 180
....*....|....*....|....*
gi 1586515037 143 VAMGRaMVREPA-AFLMDEPLSNLD 166
Cdd:PRK11819 454 LHLAK-TLKQGGnVLLLDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-215 |
2.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALR-MIAGLEEISSGTLSIGGQdvVDLAPKdrdIAMVFQSyalyphmTVFDNIA 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS--VAYVPQ---VSWIFNA-------TVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 99 FSMKLagknKAERTKRVHEIAKI---LQLEP-----LLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:PLN03232 701 FGSDF----ESERYWRAIDVTALqhdLDLLPgrdltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586515037 171 VQMRAEIASLQRQlGVTTIYVThDQTEALTMGDRVAVLKGGVLQQ 215
Cdd:PLN03232 777 HQVFDSCMKDELK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-230 |
3.90e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD--RDIAMVFQSYALYPHMTVFDNIAFS 100
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 101 MKlagkNKAERTKRVHEIakilQLEPLLGNKPAQL-----------SGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKL 169
Cdd:PLN03232 1335 EH----NDADLWEALERA----HIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 170 RVQMRAEIaslQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVNAF 230
Cdd:PLN03232 1407 DSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-194 |
5.59e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSyHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTL------SIG--GQDVVDLAPKD 75
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGyyAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 76 rdiamvfqsyalyphMTVFDNIAFSMKLAGKNKAERTkrvheiakilqlepLLG---------NKPAQ-LSGGQRQRVAM 145
Cdd:PRK15064 399 ---------------LTLFDWMSQWRQEGDDEQAVRG--------------TLGrllfsqddiKKSVKvLSGGEKGRMLF 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 146 GRAMVREPAAFLMDEPLSNLDaklrvqMRAeIASLQRQLGV---TTIYVTHD 194
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMD------MES-IESLNMALEKyegTLIFVSHD 494
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-211 |
5.61e-10 |
|
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: 58.41 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 30 GEFLILVGPSGCGKSTALRMIAGLEEIS--SGTLSIGGQdvvdlaPKD----RDIAMVFQSYALYPHMTVFDNIAFSMKL 103
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 104 AGknkaertkrvheiakilqlepllgnkpaqLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAklrvQMRAEIASLQRQ 183
Cdd:cd03232 107 RG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKK 153
|
170 180 190
....*....|....*....|....*....|..
gi 1586515037 184 LGVT--TIYVTHDQTEALTMG--DRVAVLKGG 211
Cdd:cd03232 154 LADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-166 |
7.00e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdRDIAMvFQSY--ALYPHMTVFDNI 97
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK---------LEVAY-FDQHraELDPEKTVMDNL 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 98 AfsmklAGKNKAERTKRVHEIAKILQ---LEPLLGNKPAQ-LSGGQRQRVAMGRAMVRePAAFL-MDEPLSNLD 166
Cdd:PRK11147 405 A-----EGKQEVMVNGRPRHVLGYLQdflFHPKRAMTPVKaLSGGERNRLLLARLFLK-PSNLLiLDEPTNDLD 472
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-234 |
7.55e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.58 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGnSYHAIKDLSlTIHDGEFLILVGPSGCGKSTALRMIAGLEEissgtlsiggqdvvdlaPKDRDIAmvfqsyalyph 90
Cdd:cd03222 8 KRYG-VFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLI-----------------PNGDNDE----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 mtvFDNIAFSMKlagknkaertkrvheiakilqlepllgNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLR 170
Cdd:cd03222 58 ---WDGITPVYK---------------------------PQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586515037 171 VQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKG--GVLQQVDTPKALyHRPVNAFVAGF 234
Cdd:cd03222 108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGepGVYGIASQPKGT-REGINRFLRGY 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-194 |
2.06e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 26 TIHDGEFLILVGPSGCGKSTALRMIAGL---------EEIS--------SGT--------LSIGGQDV------VDLAPK 74
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfRGTelqnyfkkLYNGEIKVvhkpqyVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 75 drdiamvfqsyalyphmtVFDniafsmklaGK-----NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAM 149
Cdd:PRK13409 175 ------------------VFK---------GKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586515037 150 VREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRqlGVTTIYVTHD 194
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-218 |
2.06e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPK---DRDIAMVFQSYALYPHMTVFD 95
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NI---AFSMK--LAGKNKAER-TKRVHEIAKIlQLEPllGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKl 169
Cdd:PRK10982 93 NMwlgRYPTKgmFVDQDKMYRdTKAIFDELDI-DIDP--RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586515037 170 RVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGvlQQVDT 218
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG--QWIAT 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-194 |
2.21e-09 |
|
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: 59.03 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 35 LVGPSGCGKSTALRMIAG------------------------------LEEISSGTL--SIGGQdVVDLAPKdrdiamvf 82
Cdd:COG1245 104 ILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelqdyFKKLANGEIkvAHKPQ-YVDLIPK-------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 83 qsyalyphmtVFDniafsmklaGK-----NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL 157
Cdd:COG1245 175 ----------VFK---------GTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586515037 158 MDEPLSNLDAKLRVQMraeiASLQRQL---GVTTIYVTHD 194
Cdd:COG1245 236 FDEPSSYLDIYQRLNV----ARLIRELaeeGKYVLVVEHD 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-214 |
3.36e-09 |
|
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: 58.30 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS-SGTLSIGGQDVVDLAPKD---RDIAMVFQS---YALYPHMT 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSM--KLAGKNKAERTKRVHEIAKILQLEPLLGNKP----AQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:TIGR02633 356 VGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 167 aklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQ 214
Cdd:TIGR02633 436 ----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-229 |
5.28e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 107 NKAERTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQlGV 186
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1586515037 187 TTIYVTHDQTEA------LTMGDRVAVLKGGVLQQVDTP---KALYHRPVNA 229
Cdd:NF000106 196 TVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggRTLQIRPAHA 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-194 |
6.02e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTlsiggqdvVDLAPKDRdIAMVFQSYALYPH 90
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGIK-VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 91 MTVFDNI-------------------AFSMKLAGKNK-AERTKRVHEI----------------AKILQLEPllGNKP-A 133
Cdd:PRK11819 85 KTVRENVeegvaevkaaldrfneiyaAYAEPDADFDAlAAEQGELQEIidaadawdldsqleiaMDALRCPP--WDAKvT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586515037 134 QLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKlrvqmraEIASLQRQL----GvTTIYVTHD 194
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLhdypG-TVVAVTHD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-211 |
6.43e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDRD---IAMVFQSYALYPHMTVFD 95
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 96 NIAFSMKLAGKNKAERTKRVHEIA-KILQL-------EPLLGnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNL-- 165
Cdd:PRK10762 99 NIFLGREFVNRFGRIDWKKMYAEAdKLLARlnlrfssDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtd 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586515037 166 ---DAKLRVqmraeIASLQRQlGVTTIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK10762 175 tetESLFRV-----IRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-211 |
1.04e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGleEISSGTLSIGGQDVVDLAPKDRDIAMV-----FQSYALYPHMTVf 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVTLNGEPLAAIdaprlARLRAVLPQAAQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 DNIAFSMK---LAG-----KNKAERTKRVHEIA-KILQL---EPLLGNKPAQLSGGQRQRVAMGRAM---------VREP 153
Cdd:PRK13547 94 PAFAFSAReivLLGryphaRRAGALTHRDGEIAwQALALagaTALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 154 AAFLMDEPLSNLDAKLRVQMRAEIASLQR--QLGVTTIyvTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAI--VHDPNLAARHADRIAMLADG 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-166 |
1.08e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLE--EISSGTLSIGGQDVVDLAPKDR---DIAMVFQsyalYPhmtvf 94
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YP----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 95 dniafsMKLAG-KNKAERTKRVHEIAKILQLEPL--------------LGNKPAQL---------SGGQRQRVAMGRAMV 150
Cdd:PRK09580 88 ------VEIPGvSNQFFLQTALNAVRSYRGQEPLdrfdfqdlmeekiaLLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
|
170
....*....|....*.
gi 1586515037 151 REPAAFLMDEPLSNLD 166
Cdd:PRK09580 162 LEPELCILDESDSGLD 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-214 |
1.11e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGL-EEISSGTLSIGGQDVVDLAPKD---RDIAMVFQS---YALYPHMT 92
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSM--KLAGK---NKAERTKRVHEIAKILQLE---PLLgnKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSN 164
Cdd:PRK13549 358 VGKNITLAAldRFTGGsriDDAAELKTILESIQRLKVKtasPEL--AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 165 LDaklrVQMRAEIASLQRQL---GVTTIYVTHDQTEALTMGDRVAVLKGGVLQ 214
Cdd:PRK13549 436 ID----VGAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-145 |
1.16e-08 |
|
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: 56.73 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 23 LSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDlapKDRD-----IAMVFQSYALyphmtvFDni 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREayrqlFSAVFSDFHL------FD-- 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586515037 98 afsmKLAGKNKAERTKRVHEIAKILQLEpllgNKPA---------QLSGGQRQRVAM 145
Cdd:COG4615 420 ----RLLGLDGEADPARARELLERLELD----HKVSvedgrfsttDLSQGQRKRLAL 468
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-211 |
1.37e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 30 GEFLILVGPSGCGKSTALRMIAglEEISSGTLSiGGQDVVDLAPKD----RDIAMVFQSYALYPHMTVFDNIAFSMKLAG 105
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 106 KN---KAERTKRVHEIAKILQLE----PLLGNKPAQLSGGQRQRVAMGRAMVREPAAFL-MDEPLSNLDAklrvQMRAEI 177
Cdd:TIGR00956 866 PKsvsKSEKMEYVEEVIKLLEMEsyadAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS----QTAWSI 941
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586515037 178 ASLQRQLGVT--TIYVTHDQTEALTMG--DRVAVL-KGG 211
Cdd:TIGR00956 942 CKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLqKGG 980
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-216 |
1.67e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIA----GLEEISSGTLSIGGQDVVDLAPKDR-DIAMVFQSY 85
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 86 ALYPHMTVFDNIAFSMKLAGKN--------KAERTKRVHEIAKILQL----EPLLGNKPAQ-LSGGQRQRVAMGRAMVRE 152
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTPQnrpdgvsrEEYAKHIADVYMATYGLshtrNTKVGNDFVRgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 153 PAAFLMDEPLSNLDAKLRVQMraeIASLQRQLGV--TTIYVTHDQT--EALTMGDRVAVLKGGvlQQV 216
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEF---IRALKTSANIldTTPLVAIYQCsqDAYELFDKVIVLYEG--YQI 290
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-235 |
3.20e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 11 KTYGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE----ISSGTLSIGGQDVVDLAPKDR------DIAM 80
Cdd:PRK15093 14 KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 81 VFQ--SYALYPHMTVFDNIAFS----------MKLAGKNKAERTKRVHEIAkILQLEPLLGNKPAQLSGGQRQRVAMGRA 148
Cdd:PRK15093 94 IFQepQSCLDPSERVGRQLMQNipgwtykgrwWQRFGWRKRRAIELLHRVG-IKDHKDAMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 149 MVREPAAFLMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKALYHRPVN 228
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
....*..
gi 1586515037 229 AFVAGFI 235
Cdd:PRK15093 253 PYTQALI 259
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-222 |
3.40e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKDrdiamvfqsyaLYPHMTVF--DNI 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-----------LRFKITIIpqDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 98 AFSMKLAGKNKAERTKRVHEIAKILQLEPLLGNKPAQ--------------LSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:TIGR00957 1371 LFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586515037 164 NLDAKLRVQMRAEIASlqrQLGVTTIYVTHDQTEALTMGDRVAVLKGGVLQQVDTPKAL 222
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRT---QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-289 |
4.97e-08 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 48.59 E-value: 4.97e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1586515037 241 NLFEGRLASGRIHLPGFSIPlsggalerAPGLSAFEGKDVIFGVRPEDL 289
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALP--------LPELAGAEGSEVVAYVRPHDL 41
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-166 |
2.59e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 21 KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTlsiggqdvVDLAPKDRdIAmVFQSYalypHMTVFD---NI 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT--------VFRSAKVR-MA-VFSQH----HVDGLDlssNP 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 98 AFSMKLAGKNKAERTKRVH----EIAKILQLEPLLgnkpaQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PLN03073 592 LLYMMRCFPGVPEQKLRAHlgsfGVTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-208 |
4.32e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 24 SLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGT----------LSIGG-QDVVDLAPKDRDIAMvfqsyaLYPHMT 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFEQlQKLVSDEWQRNNTDM------LSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFSMKLAGKNKAERtkrVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQ 172
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPAR---CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586515037 173 MRAEIASLQRQlGVTTIYVTHDQTEALTMGDRVAVL 208
Cdd:PRK10938 174 LAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-211 |
5.31e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 19 AIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDLAPKD---RDIAMVFQ---SYALYPHMT 92
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 V-FDNIAFSMK--------LAGKNKAERTKRVHEIAKILQlePLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK10982 343 IgFNSLISNIRnyknkvglLDNSRMKSDTQWVIDSMRVKT--PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586515037 164 NLD--AKLRV-QMRAEIAslQRQLGVttIYVTHDQTEALTMGDRVAVLKGG 211
Cdd:PRK10982 421 GIDvgAKFEIyQLIAELA--KKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-166 |
7.58e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 15 NSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLE--EISSGTLSIGGQDVVDLAPKDRD---IAMVFQsyalYP 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 90 -HMTVFDNIAF----------SMKLAGKNKAERTKRVHEIAKILQLEP--LLGNKPAQLSGGQRQRVAMGRAMVREPAAF 156
Cdd:CHL00131 94 iEIPGVSNADFlrlaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELA 173
|
170
....*....|
gi 1586515037 157 LMDEPLSNLD 166
Cdd:CHL00131 174 ILDETDSGLD 183
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
16-194 |
1.25e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 16 SYHaiKDLSLTIHDGEFLIlVGPSGCGKSTalrMIAGLEEISSGTL---SIGGQDVVDLAPKDRDIAMV---FQS----- 84
Cdd:cd03240 11 SFH--ERSEIEFFSPLTLI-VGQNGAGKTT---IIEALKYALTGELppnSKGGAHDPKLIREGEVRAQVklaFENangkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 85 YALYPHMTVFDNIAFsmklagknkaertkrVH--EIAKILQLEpllgnkPAQLSGGQRQ------RVAMGRAM-VREPAA 155
Cdd:cd03240 85 YTITRSLAILENVIF---------------CHqgESNWPLLDM------RGRCSGGEKVlasliiRLALAETFgSNCGIL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586515037 156 FLmDEPLSNLDA-KLRVQMRAEIASLQRQLGVTTIYVTHD 194
Cdd:cd03240 144 AL-DEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-222 |
6.53e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.21 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 4 VVLDKICKTYGNSYHAI-KDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQDVVDL---APKDRdIA 79
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 80 MVFQsyalyphmtvfDNIAFSMKLAGKNKAERT---KRVHEIAKILQLEPLLGNKPAQL-----------SGGQRQRVAM 145
Cdd:cd03288 99 IILQ-----------DPILFSGSIRFNLDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586515037 146 GRAMVREPAAFLMDEPLSNLD-AKLRVQMRAEIASLQRQLGVTTIYVTHDQTEAltmgDRVAVLKGGVLQQVDTPKAL 222
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDmATENILQKVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENL 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-196 |
8.88e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 13 YGNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRmiAGLEEIssgtlsiGGQDVVDLAPKdrdiamvfqsyaLYPHMT 92
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS-------GKARLISFLPK------------FSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VF-DNIAFSMKLAgknkaertkrvheiakilqLEPL-LGNKPAQLSGGQRQRVAMGRAMVREP--AAFLMDEPLSNLDAK 168
Cdd:cd03238 63 IFiDQLQFLIDVG-------------------LGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*...
gi 1586515037 169 LRVQMRAEIASLqRQLGVTTIYVTHDQT 196
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHNLD 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
9.08e-06 |
|
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: 45.06 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 30 GEFLILVGPSGCGKSTALRMIAGLeeissgtlsiggqdvvdLAPKDRDIAMVfqsyalyphmtvfdniafsmklagknka 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-----------------LGPPGGGVIYI---------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 110 eRTKRVHEIAKILQLEPLLGNKPAQLSGGQRQRVAMGRAMVREPAAFLMDEPLSNLDAKLRVQMRAEI-----ASLQRQL 184
Cdd:smart00382 37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180
....*....|....*....|
gi 1586515037 185 GVTTIYVTHDQTEALTMGDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-198 |
1.75e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEIS-SGTLSI------GGQDVVDLapkDRDIAMVfqSYALypHM- 91
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLfgrrrgSGETIWDI---KKHIGYV--SSSL--HLd 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 92 -----TV--------FDNIAFSMKLAGKNKaertKRVHEIAKILQLEPLLGNKPAQ-LSGGQRQRVAMGRAMVREPAAFL 157
Cdd:PRK10938 349 yrvstSVrnvilsgfFDSIGIYQAVSDRQQ----KLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586515037 158 MDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIYVTHDQTEA 198
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-175 |
2.08e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEE--ISSGTLSIGGqdvvdlAPKDRDIAMVFQSYALY-----PHMT 92
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG------FPKKQETFARISGYCEQndihsPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 93 VFDNIAFS--MKLAGK-NKAERTKRVHEIAKILQLEPLlgnKPA--------QLSGGQRQRVAMGRAMVREPAAFLMDEP 161
Cdd:PLN03140 970 VRESLIYSafLRLPKEvSKEEKMMFVDEVMELVELDNL---KDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170
....*....|....*
gi 1586515037 162 LSNLDAK-LRVQMRA 175
Cdd:PLN03140 1047 TSGLDARaAAIVMRT 1061
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-163 |
2.09e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 14 GNSYHAIKDLSLTIHDGEFLILVGPSGCGKSTALRMIAGLEEISSGTLSIGGQdvvdlapkdrdIAMVFQSYALYPHMTV 93
Cdd:PRK13545 34 GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586515037 94 FDNIAFS---MKLAGKNKAERTKRVHEIAKILQLEpllgNKPAQ-LSGGQRQRVAMGRAMVREPAAFLMDEPLS 163
Cdd:PRK13545 103 IENIELKglmMGLTKEKIKEIIPEIIEFADIGKFI----YQPVKtYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
136-230 |
1.03e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 136 SGGQRQRVAMGRAMVREPAAF-LMDEPLSNLDAKLRVQMRAEIASLQRQLGVTTIyvTHdQTEALTMGDRVAVLKGGVLQ 214
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFiLMDEATANIDPALDRQIQATVMSAFSAYTVITI--AH-RLHTVAQYDKIIVMDHGAVA 1523
|
90
....*....|....*.
gi 1586515037 215 QVDTPKALYHRPVNAF 230
Cdd:PTZ00243 1524 EMGSPRELVMNRQSIF 1539
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
283-373 |
1.41e-04 |
|
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: 39.91 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 283 GVRPEDLydsRLPSGAShpTIPGVVKSIEELGSELIVHlkidaVRIDSGDPDAVEDLSGAANAVARfeavsavetGQSID 362
Cdd:pfam08402 2 AIRPEKI---RLAAAAN--GLSGTVTDVEYLGDHTRYH-----VELAGGEELVVRVPNAHARPPAP---------GDRVG 62
|
90
....*....|.
gi 1586515037 363 LAIDPAKLHFF 373
Cdd:pfam08402 63 LGWDPEDAHVL 73
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-166 |
1.99e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 20 IKDLSLTIHDGEFLILVGPSGCGKSTALRMIA-----GLE---EISSGTLSIGGQDVVDL-APKDRDI---------AMV 81
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPkncQILHVEQEVVGDDTTALqCVLNTDIertqlleeeAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586515037 82 FQSYALYPHMTVFDNIAFSMKlAGKNKAERTKRVHEIAKILQL-----------EPLLG---------NKPAQLSGGQRQ 141
Cdd:PLN03073 273 VAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLELidaytaearaaSILAGlsftpemqvKATKTFSGGWRM 351
|
170 180
....*....|....*....|....*
gi 1586515037 142 RVAMGRAMVREPAAFLMDEPLSNLD 166
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
134-192 |
9.63e-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: 9.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586515037 134 QLSGGQRQRVAMGR--AMVR-EPAAF-LMDEPLSNLDAklrvQMRAEIASLQRQLGVTTIYVT 192
Cdd:cd03272 158 QLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDA----QYRTAVANMIKELSDGAQFIT 216
|
|
| |
