|
Name |
Accession |
Description |
Interval |
E-value |
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-372 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 780.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA 80
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ENRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 160
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 161 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVAS 240
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 241 FIGEINLFNATVIERLDEQRVRASVEGRECNIYVNFPVERGQRLNVLLRPEDLRVDEVHDGSDADGLIGYIRERNYKGMT 320
Cdd:PRK09452 244 FIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490998897 321 LESVVELENGKMVMVSEFFNEDDPDFDHPLDQKMAINWVESWEVVLADEEHK 372
Cdd:PRK09452 324 LDSVVELENGKMVMVSEFFNEDDPDFDHSLGQKVAVTWVEGWEVVLADEEHK 375
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-366 |
0e+00 |
|
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: 547.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 42 LLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPR 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 122 VLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 201
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 202 QEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLFNATVIERLDEQRVRASVEGRECNIYVNFPVERG 281
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 282 QRLNVLLRPEDLRVDEVHDGSDADGLIGYIRERNYKGMTLESVVELENGKMVMVSEFFNEDDPDFDHPLDQKMAINWVES 361
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPG 320
|
....*
gi 490998897 362 WEVVL 366
Cdd:TIGR01187 321 SEVVL 325
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-368 |
0e+00 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 529.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTV 88
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 169 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLF 248
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 249 NATVIERLDEqrvRASVEGRECNIYVNFPVERGQRLNVLLRPEDLRvdeVHDGSDADGLIGYIRERNYKGMTLESVVELE 328
Cdd:COG3842 243 PGTVLGDEGG---GVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIR---LSPEGPENGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490998897 329 NGKMVMVSEFFNEDDPdfdHPLDQKMAINWVESWEVVLAD 368
Cdd:COG3842 317 DGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-302 |
5.33e-153 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 434.89 E-value: 5.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE--INLFN 249
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 250 ATVIE---RLDEQRVRASVEGRecniyvnfpVERGQRLNVLLRPEDLRVDEVHDGS 302
Cdd:COG3839 244 GTVEGggvRLGGVRLPLPAALA---------AAAGGEVTLGIRPEHLRLADEGDGG 290
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-243 |
5.61e-149 |
|
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: 420.10 E-value: 5.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIG 243
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-304 |
2.53e-132 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 382.19 E-value: 2.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI-THVPAENRHVNTVFQ 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLFNA 250
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 251 TVIerldEQRVRASvegrECNIYVNFPVERGQRLnVLLRPEDLRVDEVHDGSDA 304
Cdd:COG1118 243 RVI----GGQLEAD----GLTLPVAEPLPDGPAV-AGVRPHDIEVSREPEGENT 287
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-329 |
2.86e-121 |
|
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: 354.34 E-value: 2.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNT 87
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINL 247
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 248 FNAtviERLDEQRVRASVEGRECNIYVnfpVERGQRLNVLLRPEDLRvdeVHDGSDADGLI-GYIRERNYKGMTLESVVE 326
Cdd:TIGR03265 241 LPG---TRGGGSRARVGGLTLACAPGL---AQPGASVRLAVRPEDIR---VSPAGNAANLLlARVEDMEFLGAFYRLRLR 311
|
...
gi 490998897 327 LEN 329
Cdd:TIGR03265 312 LEG 314
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-224 |
5.93e-119 |
|
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: 342.96 E-value: 5.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-294 |
6.92e-112 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 330.65 E-value: 6.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKT-VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAEnRHVNTVF 89
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 170 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE--INL 247
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490998897 248 FNATVieRLDEQRVRASvEGRECNIYVNFPVERGQRLNVLLRPEDLR 294
Cdd:PRK11650 243 LDGRV--SADGAAFELA-GGIALPLGGGYRQYAGRKLTLGIRPEHIA 286
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-224 |
3.75e-110 |
|
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: 320.74 E-value: 3.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-342 |
4.99e-110 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 325.52 E-value: 4.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLFNAT 251
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 252 vierLDEQRVrasvegrecNIY---------VNFPVERGQRLnVLLRPEDLRVDEvhDGSDADGLIgyIRERNYKGMTLE 322
Cdd:PRK11432 247 ----LSGDYV---------DIYgyrlprpaaFAFNLPDGECT-VGVRPEAITLSE--QGEESQRCT--IKHVAYMGPQYE 308
|
330 340
....*....|....*....|...
gi 490998897 323 SVVELeNGKMVMV---SEFFNED 342
Cdd:PRK11432 309 VTVDW-HGQELLLqvnATQLQPD 330
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-244 |
5.40e-109 |
|
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: 318.90 E-value: 5.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQK----TPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 244
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-333 |
9.14e-109 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 323.33 E-value: 9.14e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH 84
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 244
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 245 INLFNATVIERLDEQRVRASvEGRECNIYVN--FPVERGQRLNVLLRPEDLRV-DEV-HDGSD-ADGLIGYIRernYKGM 319
Cdd:PRK11607 253 VNVFEGVLKERQEDGLVIDS-PGLVHPLKVDadASVVDNVPVHVALRPEKIMLcEEPpADGCNfAVGEVIHIA---YLGD 328
|
330
....*....|....
gi 490998897 320 TLESVVELENGKMV 333
Cdd:PRK11607 329 LSIYHVRLKSGQMI 342
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-252 |
1.02e-100 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 302.00 E-value: 1.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRM----QKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINL 247
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 490998897 248 FNATV 252
Cdd:PRK10851 243 LQGTI 247
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-223 |
1.04e-99 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 295.85 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSF----DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENRHV 85
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKIEQD 223
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-293 |
1.08e-96 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 292.32 E-value: 1.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFdGKTVIS-DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQ 90
Cdd:PRK11000 4 VTLRNVTKAY-GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIG--EINLF 248
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 249 NATV---------IERLDEQRVRASVEGREcniyvnfpVERGQRLNVLLRPEDL 293
Cdd:PRK11000 243 PVKVtataieqvqVELPNRQQVWLPVEGRG--------VQVGANMSLGIRPEHL 288
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-220 |
3.46e-95 |
|
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: 282.82 E-value: 3.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENRHVNT 87
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKI 220
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-247 |
1.06e-88 |
|
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: 266.89 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQSYALFPHMSVFENVA 105
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 106 FGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 185
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 186 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINL 247
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-294 |
6.31e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 265.43 E-value: 6.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTV-ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE------NRHVNTVFQSYALF 95
Cdd:COG4175 38 GQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:COG4175 118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 176 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEIN---LFNA-- 250
Cdd:COG4175 198 IRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDrskVLTAgs 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490998897 251 ------TVIERLDEQRVrASVEGRECNIYVNFPVERGQRLNVLLRPEDLR 294
Cdd:COG4175 278 vmrppeAVVSEKDGPRV-ALRRMREEGISSLYVVDRDRRLLGVVTADDAL 326
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-244 |
2.41e-84 |
|
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: 256.07 E-value: 2.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTV 88
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 167 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 244
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-223 |
7.34e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 254.20 E-value: 7.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSF-DGK---TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE--- 81
Cdd:COG1136 2 SPLLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 ---NRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 158
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 159 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGKIEQD 223
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-234 |
8.71e-82 |
|
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: 258.68 E-value: 8.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGK-----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN- 82
Cdd:COG1123 258 EPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 ----RHVNTVFQ--SYALFPHMSVFENVAFGLRMQKT-PAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIAR 154
Cdd:COG1123 338 relrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-242 |
2.05e-81 |
|
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: 249.48 E-value: 2.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN------RHVNTVFQ 90
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 242
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-242 |
1.65e-79 |
|
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: 243.73 E-value: 1.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-----NRH 84
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYALFPHMSVFENVAFGLRMQKT-PAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 163
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 164 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIyEEPKNLFVASFI 242
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-220 |
7.32e-78 |
|
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: 238.54 E-value: 7.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDG----KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE------ 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 NRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-235 |
1.64e-77 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 238.36 E-value: 1.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE----NRHVN 86
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFGLRM-QKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 166 DESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 235
Cdd:COG1126 161 DEPTSALD----PELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-311 |
1.37e-75 |
|
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: 237.83 E-value: 1.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 19 KSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAENRHVN-----TVFQSY 92
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRrkkigMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 173 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLFNATV 252
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 253 IERLDEqrvrasvegRECNIYVNFPVERGQRLNVLLRpEDLRVDEVHDGSDADGLIGYI 311
Cdd:TIGR01186 241 AERIAQ---------RMNTGPITKTADKGPRSALQLM-RDERVDSLYVVDRQNKLVGVV 289
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-236 |
2.24e-73 |
|
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: 227.60 E-value: 2.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQS--YALFpH 97
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 178 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-229 |
3.69e-73 |
|
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: 227.38 E-value: 3.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAENRHVNT--- 87
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLRRrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 -VFQSYALFPHMSVFENVAFGLRMQ-KTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:cd03261 81 mLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-219 |
3.76e-72 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 222.45 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT----HVPAENRHVNT 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVAFGLrmqktpaaeitprvldalrmvqleefaqrkphqlSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-242 |
8.03e-72 |
|
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: 224.30 E-value: 8.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSF----DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP--AENRH 84
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSY--ALFPHMSVFENVAFGLRMQKTPaaEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN-----L 236
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHpytreL 238
|
....*.
gi 490998897 237 FVASFI 242
Cdd:COG1124 239 LAASLA 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-224 |
8.49e-72 |
|
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: 222.94 E-value: 8.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 14 LAGIRKSFDGKTVisDLNLTINnGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED------QDITHVPAENRHVNT 87
Cdd:cd03297 3 CVDIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVAFGLRmqKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-244 |
1.03e-71 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 223.48 E-value: 1.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 31 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQSYALFPHMSVFENVAFGLRm 110
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 111 qktPAAEITP----RVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV-NKPrLLLLDESLSALDYKLRKQMQNELK 185
Cdd:COG3840 98 ---PGLKLTAeqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 186 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 244
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-220 |
1.25e-70 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 221.66 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHvPAENRHVntVFQSYALFPHMSVFEN 103
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:COG4525 97 VAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQEL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 490998897 184 LKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGKI 220
Cdd:COG4525 177 LLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-224 |
2.75e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 216.84 E-value: 2.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHV 85
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-304 |
1.72e-68 |
|
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: 219.59 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED---QD---ITHVPAENRHVNTVFQSYALFPHMSVFE 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDsarGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGLRmqKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 182
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 183 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINLFNATVIERLDEQR-V 261
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGlT 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 262 RASVEGREcnIYVNF-PVERGQRL-------NVLL---RPEDL--------RVDEVHDGSDA 304
Cdd:COG4148 255 RLALGGGR--LWVPRlDLPPGTRVrvrirarDVSLalePPEGSsilnilpgRVVEIEPADGG 314
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-232 |
1.67e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 213.38 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----R 83
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HVNTVFQSYALFPHMSVFENVAFG-----------LRMQktPAAEItPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAI 152
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLF--PPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 153 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-224 |
4.25e-67 |
|
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: 211.60 E-value: 4.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR--- 83
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 --HVNTVFQSY--ALFPHMSVFENVAFGLRMQK--TPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAV 156
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 157 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-232 |
3.98e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.15 E-value: 3.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHVNTVFQ 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 171 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-220 |
1.31e-65 |
|
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: 207.00 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH----VPAENRHVNT 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVAFGLR-MQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 167 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-219 |
2.30e-65 |
|
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: 206.55 E-value: 2.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKT--VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTV 88
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQsyalFP-HM----SVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 163
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 164 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-268 |
1.71e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.39 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP-----AEN 82
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 162
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 163 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeealtMS------DRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260 270
....*....|....*....|....*....|..
gi 490998897 237 FVASFIGEInlFNATVIERLDEQRVRASVEGR 268
Cdd:COG1135 236 LTRRFLPTV--LNDELPEELLARLREAAGGGR 265
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-236 |
2.01e-64 |
|
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: 213.23 E-value: 2.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDG--KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL---ENVDSGRIHLEDQDITHVPAENR 83
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 --HVNTVFQS--YALFPhMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 159
Cdd:COG1123 82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 160 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-229 |
5.45e-64 |
|
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: 204.51 E-value: 5.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTV 88
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFG----LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-234 |
5.47e-62 |
|
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: 198.57 E-value: 5.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP-----AE 81
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 NRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-234 |
6.91e-62 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 201.50 E-value: 6.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFD------GKTV-----ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV 78
Cdd:COG4608 6 PLLEVRDLKKHFPvrgglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 79 PAEN-----RHVNTVFQ-SYA-LFPHMSVFENVAFGLRMQK-TPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQR 149
Cdd:COG4608 86 SGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGKIEQDGT 225
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAP 241
|
....*....
gi 490998897 226 PREIYEEPK 234
Cdd:COG4608 242 RDELYARPL 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-232 |
8.14e-61 |
|
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: 195.86 E-value: 8.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHVN 86
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFGLRMQKT---------PAAEItPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 157
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRStwrslfglfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 158 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-218 |
1.35e-57 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 187.98 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEnRHVntVFQ 90
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-RGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 218
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-242 |
2.17e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 186.84 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHV----N 86
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFG-LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 242
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-236 |
2.34e-57 |
|
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: 187.64 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI---THVPAENRHVNTVFQSyalfPH- 97
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVGMVFQN----PDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 ----MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:TIGR04520 89 qfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 174 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:TIGR04520 169 PKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-232 |
3.36e-57 |
|
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: 186.60 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHVNTVF 89
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 170 SALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-231 |
8.42e-57 |
|
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: 196.98 E-value: 8.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlrmqktpAAEITP-RVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:COG2274 565 IRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 168 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPREIYE 231
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-229 |
9.01e-57 |
|
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: 184.69 E-value: 9.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV-----DSGRIHLEDQDI----THVPAEN 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQSYALFPhMSVFENVAFGLRMQKT-PAAEITPRVLDALRMVQL-EEFAQR-KPHQLSGGQQQRVAIARAVVNK 159
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 160 PRLLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-217 |
1.32e-56 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 183.84 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD---SGRIHLEDQDITHVPAENRHVNTVFQSYALFPHM 98
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFGLRmQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 178
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 490998897 179 QMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRD 217
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-234 |
1.45e-56 |
|
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: 187.18 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE---NVDSGRIHLEDQDITHVPAEN- 82
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 -----RHVNTVFQ-SY-ALFPHMSVFENVAFGLRM-QKTPAAEITPRVLDALRMVQL---EEFAQRKPHQLSGGQQQRVA 151
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 152 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI-EQdGTPREIY 230
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEE-GPVEELF 239
|
....
gi 490998897 231 EEPK 234
Cdd:COG0444 240 ENPR 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
16-232 |
4.12e-56 |
|
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: 183.65 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHVNTVF 89
Cdd:TIGR02315 6 NLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGlRMQKTPA---------AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 160
Cdd:TIGR02315 86 QHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 161 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-228 |
5.93e-56 |
|
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: 183.02 E-value: 5.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLSPLVQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA 80
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 E------NRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEitPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 154
Cdd:COG4181 82 DararlrARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPRE 228
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-229 |
6.10e-56 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 183.70 E-value: 6.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH---- 84
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTvFQSYALFPHMSVFENVA---------------FGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQR 149
Cdd:COG0411 82 ART-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-254 |
1.01e-55 |
|
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: 186.09 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED-------QDIThVPAENRHVNTVFQSYALFPHMSVF 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIF-LPPEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGLRMQKTPAAEITPRVLdaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 181
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERV--IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 182 NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPkNLFVASFIGEINLFNATVIE 254
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP-DLPWLAREDQGSLIEGVVAE 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-223 |
2.06e-55 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 182.57 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVqLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRhvnTVF 89
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQKTPAAeitprvLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLKGQWRDAA------LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 170 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 223
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-220 |
2.24e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.78 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQ 90
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPhMSVFENVAFGLRMQKTPAAEitPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490998897 170 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-245 |
3.16e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 184.62 E-value: 3.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGK----TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP-----AEN 82
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 162
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 163 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFI 242
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
...
gi 490998897 243 GEI 245
Cdd:PRK11153 242 QST 244
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-233 |
3.80e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 178.74 E-value: 3.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVpaeNRHVNTV 88
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYAL---FPhMSVFENVAFGL----RMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEqDGTPREIYEEP 233
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-244 |
6.42e-54 |
|
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: 186.04 E-value: 6.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFDGKTV-----ISDLNLTINNGEFLTLLGPSGCGKTT----VLRLIAGlenvdSGRIHLEDQDITHVPAEN----- 82
Cdd:COG4172 287 IKRGLFRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQDLDGLSRRAlrplr 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQS-YA-LFPHMSVFENVAFGLRMQKTP--AAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVV 157
Cdd:COG4172 362 RRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 158 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI-EQdGTPREIYEEPKN- 235
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ-GPTEQVFDAPQHp 520
|
250
....*....|...
gi 490998897 236 ----LFVASFIGE 244
Cdd:COG4172 521 ytraLLAAAPLLE 533
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
1.93e-53 |
|
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: 176.50 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHvPAENRHVntVFQSYALFPHMSVFENVAF 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 GLR--MQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 184
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 185 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGtprEIYEEP 233
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
16-229 |
3.58e-53 |
|
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: 175.70 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH---VNTVFQSY 92
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENVAFGLRMQKTPA----------AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 162
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 163 LLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-224 |
6.46e-53 |
|
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: 174.60 E-value: 6.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQSYALFPHMSVFENVAFGL 108
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 109 rmqkTPAAEITP----RVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 184
Cdd:cd03298 96 ----SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490998897 185 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-255 |
3.16e-52 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 178.30 E-value: 3.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP-AENRHVN-----TVFQSYALFPHMSV 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 180
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 181 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGEINL---FNATVIER 255
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIsqvFSAKDIAR 281
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-220 |
8.17e-52 |
|
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: 170.27 E-value: 8.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR-HVNTVFQ 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVafglrmqktpaaeitprvldalrmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490998897 171 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-224 |
1.14e-51 |
|
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: 169.92 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQ 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 syalfphmsvfenvafglrmqktpaaeitprvldALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-234 |
6.33e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.19 E-value: 6.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ--DITHVPAEN------R 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HVNTVFQSYALFPHMSVFENVAFG----LRMQKTPAAEITPRVLDALRmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNK 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALARAEKLLERLR---LKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 160 PRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTpREIYEEPK 234
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-234 |
7.68e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.19 E-value: 7.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ--DITHVPAEN------R 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HVNTVFQSYALFPHMSVFEN-VAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 162
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 163 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTpREIYEEPK 234
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-219 |
4.38e-50 |
|
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: 166.89 E-value: 4.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHVNTV 88
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFGLRMQKTPAAEItpRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 169 LSALDyklrKQMQNELKAL---QRKLGITFVFVTHDQEEALtmSDRIVVMRDGK 219
Cdd:COG4133 159 FTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-220 |
4.48e-50 |
|
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: 167.20 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH-----VPAENRHVNTVFQSYALFPH 97
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 178 KQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03292 173 WEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-228 |
5.55e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 176.12 E-value: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlrmqktpAAEITP-RVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:COG1132 430 IRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 168 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-167 |
1.93e-48 |
|
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: 160.51 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH--VPAENRHVNTVFQSYALFPHMSVFENV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 105 AFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRK----PHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-219 |
7.49e-48 |
|
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: 159.33 E-value: 7.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQ 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 syalfphmsvfenvafglrmqktpaaeitprvldalrmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 171 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-229 |
1.10e-47 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 161.67 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 31 NLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQSYALFPHMSVFENVAFGLRm 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 111 qktPAAEITP----RVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 186
Cdd:PRK10771 98 ---PGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 187 LQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-215 |
1.13e-47 |
|
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: 160.78 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENRHVNTVFQSYAL---FP 96
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---KERKRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 hMSVFENVAFGL----RMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:cd03235 85 -ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 173 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 215
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-229 |
5.11e-47 |
|
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: 159.21 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSF--DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI-THVPAENRHVNTV 88
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 169 LSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-233 |
5.17e-47 |
|
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: 168.02 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 4 QPRSLSPLVQLAGIRKSFDG--KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE 81
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 N--RHVNTVFQSYALFpHMSVFENVAFGlRMQKTPAAeitprVLDALRMVQLEEFAQRKPH-----------QLSGGQQQ 148
Cdd:COG4987 406 DlrRRIAVVPQRPHLF-DTTLRENLRLA-RPDATDEE-----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 149 RVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHDQEEALTMsDRIVVMRDGKIEQDGTPR 227
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHE 554
|
....*.
gi 490998897 228 EIYEEP 233
Cdd:COG4987 555 ELLAQN 560
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
8.00e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.97 E-value: 8.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRslsPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT---- 76
Cdd:COG4598 1 MTDTAP---PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 77 ----HVPAENRHVNT-------VFQSYALFPHMSVFENVAFG-LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSG 144
Cdd:COG4598 78 rdgeLVPADRRQLQRirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 145 GQQQRVAIARAVVNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIE 221
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALD----PELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
250
....*....|...
gi 490998897 222 QDGTPREIYEEPK 234
Cdd:COG4598 234 EQGPPAEVFGNPK 246
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-219 |
4.02e-46 |
|
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: 155.23 E-value: 4.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVafglrmqktpaaeitprvldalrmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 179
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490998897 180 MQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGK 219
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-236 |
4.38e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 159.06 E-value: 4.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE----NRHVNTVFQ--SYALFPH 97
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 mSVFENVAFGLRMQKTPAAEITPRVLDALRMVQL--EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 176 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-232 |
4.80e-46 |
|
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: 165.32 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlRMQKTPAAeitprVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG4988 427 IRENLRLG-RPDASDEE-----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 169 LSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-231 |
5.90e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 158.64 E-value: 5.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH--VPAENRHVNTVFQSY-ALFPHMSVFENVA 105
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQNPdNQFVGATVQDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 106 FGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 185
Cdd:PRK13635 105 FGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490998897 186 ALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYE 231
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-225 |
1.35e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 157.16 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 3 IQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN 82
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 -----RHVNTVFQSY--ALFPHMSVFENVAFGLR-MQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIA 153
Cdd:PRK10419 84 rkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 225
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-243 |
1.50e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.45 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI----------THVPAE 81
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 NRHVNTVFQSYALFPHMSVFENVAFG-LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 160
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 161 RLLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN---- 235
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtr 241
|
....*...
gi 490998897 236 LFVASFIG 243
Cdd:PRK11264 242 QFLEKFLL 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-229 |
2.91e-45 |
|
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: 154.84 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHVNTVFQ 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 171 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
26-229 |
3.73e-45 |
|
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: 154.51 E-value: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE---NRHVNTVFQSYALFPHMSVFE 102
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGLRMQKTPAAEITP-RVLDalRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 181
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYE--LFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 182 NELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03224 173 EAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-234 |
6.41e-45 |
|
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: 154.24 E-value: 6.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH---VNTVFQSY 92
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 173 DYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:cd03218 165 DPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-228 |
2.39e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 153.73 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR-HVNTVF-QSYAL-FP 96
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVLpQHSSLaFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 hMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARA-------VVNKPRLLLLDESL 169
Cdd:COG4559 90 -FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 170 SALDykLRKQmQNELKALqRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:COG4559 169 SALD--LAHQ-HAVLRLA-RQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
2.50e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 153.65 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLEnVdSGRIHLEDQ 73
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR-V-EGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 74 DI----THVPAENRHVNTVFQSYALFPhMSVFENVAFGLRMQ-KTPAAEITPRVLDALRMVQL-EEFAQR--KP-HQLSG 144
Cdd:COG1117 79 DIydpdVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwDEVKDRlkKSaLGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 145 GQQQRVAIARAVVNKPRLLLLDESLSALD-----------YKLRKQMqnelkalqrklgiTFVFVTHDQEEALTMSDRIV 213
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTA 224
|
250 260
....*....|....*....|..
gi 490998897 214 VMRDGKIEQDGTPREIYEEPKN 235
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTNPKD 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
27-230 |
2.51e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 154.12 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT--HVPAENRHVNTVFQSY-ALFPHMSVFEN 103
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490998897 184 LKALQRKLGITFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIY 230
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-220 |
4.18e-44 |
|
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: 153.42 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHVNTVFQ-SYALF-P 96
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 HMSVFENVAFGLR-MQKTPAAEITPRVLDALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490998897 175 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-234 |
2.31e-43 |
|
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: 157.54 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDG----KTVISDLNLTINNGEFLTLLGPSGCGKT----TVLRLIAGLENVDSGRIHLEDQDITHVP- 79
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 80 AENRHVN-----TVFQ--SYALFPHMSVFENVAFGLRM-QKTPAAEITPRVLDALRMVQLEEFAQR---KPHQLSGGQQQ 148
Cdd:COG4172 84 RELRRIRgnriaMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 149 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLT----MSDRIVVMRDGKIEQDG 224
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQG 239
|
250
....*....|
gi 490998897 225 TPREIYEEPK 234
Cdd:COG4172 240 PTAELFAAPQ 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
16-234 |
4.74e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.79 E-value: 4.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPaenrhvntVFQ----- 90
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--------MHKrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 -SY-----ALFPHMSVFENVAFGLRMQKTPAAEITPRvLDALrmvqLEEF-----AQRKPHQLSGGQQQRVAIARAVVNK 159
Cdd:COG1137 80 iGYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREER-LEEL----LEEFgithlRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 160 PRLLLLDESLSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-234 |
5.87e-42 |
|
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: 146.67 E-value: 5.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA-------- 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ----ENRHVntvfqsyalFPHMSVFEN--VAFGLRMQKTPAAEITPRVLDalRMVQLEEFAQRKPHQLSGGQQQRVAIAR 154
Cdd:COG0410 81 gyvpEGRRI---------FPSLTVEENllLGAYARRDRAEVRADLERVYE--LFPRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-232 |
5.98e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 147.93 E-value: 5.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED---QDITHVPAENRHVNTVFQSyalfPHMS- 99
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 ----VFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:PRK13633 99 vatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 176 LRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-224 |
9.85e-42 |
|
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: 145.41 E-value: 9.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGeFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR-HVNTVFQ 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490998897 171 ALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-220 |
1.64e-41 |
|
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: 144.67 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVFQS 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITpRVLDalrMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRID-EVLD---VVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 172 LDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-229 |
2.40e-41 |
|
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: 145.61 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGlEN--VDSGRIHLEDQDITHV-PAENR-- 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLppTYGNDVRLFGERRGGEdVWELRkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 --HVNTVFQSYaLFPHMSVFENVAFGL-----RMQKTPAAEITpRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 156
Cdd:COG1119 80 igLVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 157 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-231 |
2.54e-41 |
|
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: 145.07 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGLRmqktpaaEITP-RVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03251 92 VAENIAYGRP-------GATReEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 168 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYE 231
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-228 |
3.11e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 145.30 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNT 87
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYAL-FPhMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV------NKP 160
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 161 RLLLLDESLSALDykLRKQMQ--NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:PRK13548 160 RWLLLDEPTSALD--LAHQHHvlRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-235 |
5.22e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 144.98 E-value: 5.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKT---------VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP 79
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 80 AENR--HVNTVFQ--SYALFPHMSVFENVAFGLRMQ-KTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIA 153
Cdd:COG4167 82 YKYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
..
gi 490998897 234 KN 235
Cdd:COG4167 242 QH 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-224 |
1.93e-40 |
|
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: 142.34 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDG--KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAE-NRHVNT 87
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFpHMSVFENVAFGLrmqktPAAEiTPRVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAV 156
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 157 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQeEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-261 |
2.61e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 143.30 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSF-----DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR--H 84
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYAL--FPHMSVFENVA--------FGLRmqktpaaeitPRVLDALRmvqlEEFAQR--------------KPH 140
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLR----------RGLTKKRR----ELFRELlatlglglenrldtKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 141 QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKlRKQMQNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490998897 220 IEQD--GtpreiyEEPKNLFVASFigeINLFNATVIERLDEQRV 261
Cdd:COG1101 227 IILDvsG------EEKKKLTVEDL---LELFEEIRGEELADDRL 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-301 |
1.12e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 147.09 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH---VPAENRHVN 86
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrspRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFGlRMQKTPA----AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRL 162
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLG-REPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 163 LLLDESLSALDYK----LRKQMqNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGKieqdgtpreiyeepknlFV 238
Cdd:COG1129 162 LILDEPTASLTEReverLFRII-RRLKA----QGVAIIYISHRLDEVFEIADRVTVLRDGR-----------------LV 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 239 ASFigeinlfnatVIERLDEQR-VRASVeGREcnIYVNFPVERGQRLNVLLRPEDLRVDEVHDG 301
Cdd:COG1129 220 GTG----------PVAELTEDElVRLMV-GRE--LEDLFPKRAAAPGEVVLEVEGLSVGGVVRD 270
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-224 |
1.98e-39 |
|
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: 139.43 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKT----VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHV 85
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 166 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-220 |
4.00e-39 |
|
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: 136.79 E-value: 4.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDithvpaenrhvntvfqs 91
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 yalfphmsvfenVAFGlrmqktpaaeiTPRvlDALR----MVqleefaqrkpHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03216 64 ------------VSFA-----------SPR--DARRagiaMV----------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-225 |
5.31e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 138.80 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSF-DGKT---VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA---- 80
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 --ENRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 158
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 159 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGKIEQDGT 225
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-232 |
7.37e-39 |
|
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: 138.44 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT--HVPAENRHVNTVFQSYALFPhMSVFEN 103
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGlrmqKTPAAEITprVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:cd03249 97 IRYG----KPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 173 DYKLRKQMQnelKALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:cd03249 171 DAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-234 |
1.11e-38 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 141.00 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH-----VNTVFQS--YALFPHMS 99
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGLRM--QKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 177 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-233 |
3.73e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 137.59 E-value: 3.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIthvPAENRH------ 84
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 --VNTVFQSYALFPHMSVFENVAFGLRMQ-KTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-220 |
1.12e-37 |
|
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: 134.72 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvPAENRHVNTVFQS 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 172 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-239 |
1.30e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.27 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAEN-----RHVNTVFQSY-ALFPH 97
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENlkeirKKIGIIFQNPdNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:PRK13632 99 ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 178 KQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVA 239
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-233 |
1.75e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 138.08 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ---DI---THVPAENRHVNTVFQSYALFPHMSVFE 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGlrMQKTPAAEItprvLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 182
Cdd:PRK11144 96 NLRYG--MAKSMVAQF----DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490998897 183 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-236 |
2.97e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.59 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH----VPAENRHVNTVFQSY--ALF 95
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkksLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PHmSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 176 LRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-225 |
3.28e-37 |
|
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: 134.19 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR---HVNTVF 89
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDaLRMVqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 170 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 225
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-236 |
7.78e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 134.76 E-value: 7.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT------HVPAENRHVNTVFQsyalFPHMSVFE 102
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 -----NVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK13634 101 etvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 177 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-261 |
8.36e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.54 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHVNTVFQSY-ALFPH 97
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdirEKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 178 KQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPREIYEEPknlfvaSFIGEINL---FNATVIE 254
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV------EMLKEIGLdipFVYKLKN 252
|
....*..
gi 490998897 255 RLDEQRV 261
Cdd:PRK13640 253 KLKEKGI 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-261 |
9.16e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 9.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHvpaenRHVNTVfqS 91
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRI--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 Y-----ALFPHMSVFENVAF-----GLrmqktPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE-PKNLFVAS 240
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228
|
250 260
....*....|....*....|....*
gi 490998897 241 FIGEI----NLFNATVIERLDEQRV 261
Cdd:COG4152 229 ADGDAgwlrALPGVTVVEEDGDGAE 253
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
16-234 |
1.15e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 132.78 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH---VNTVFQSY 92
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENVAFGL-RMQKTPAAEITPRvLDALrmvqLEEF-----AQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:TIGR04406 86 SIFRKLTVEENIMAVLeIRKDLDRAEREER-LEAL----LEEFqishlRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 167 ESLSALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLkERGIG---VLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-293 |
1.15e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 135.73 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPL-VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDithVP 79
Cdd:PRK13536 30 KASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 80 AENR----HVNTVFQSYALFPHMSVFEN-VAFG--LRMQKTPAAEITPRVLDALRmvqLEEFAQRKPHQLSGGQQQRVAI 152
Cdd:PRK13536 107 ARARlaraRIGVVPQFDNLDLEFTVRENlLVFGryFGMSTREIEAVIPSLLEFAR---LESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 153 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 233 PKNLFVASFIGEiNLFNATVIERLDEQRVRASVEGRECniYVNFPVE-----RGQR-LNVLLRPEDL 293
Cdd:PRK13536 263 HIGCQVIEIYGG-DPHELSSLVKPYARRIEVSGETLFC--YAPDPEQvrvqlRGRAgLRLLQRPPNL 326
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-236 |
1.47e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 133.34 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQS-YALFPHM 98
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 178
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 179 QMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-220 |
1.99e-36 |
|
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: 131.23 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDItHVPAENRHVNTVFQS--YALFPHmS 99
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGLRmqktPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 179
Cdd:cd03226 89 VREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490998897 180 MQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03226 165 VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-231 |
3.52e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.39 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLSPLvQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI-THVPAENR 83
Cdd:PRK13537 2 PMSVAPI-DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 163
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 164 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 231
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-228 |
6.81e-36 |
|
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: 130.81 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMS 99
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlrmqKTPAAEItpRVLDALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:cd03253 91 IGYNIRYG----RPDATDE--EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 169 LSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPRE 228
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-233 |
1.46e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 130.50 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RH--V 85
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMgvV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTvFQSYALFPHMSVFEN--VAFGLRMQ--------KTPA-----AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRV 150
Cdd:PRK11300 84 RT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 151 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 230
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 490998897 231 EEP 233
Cdd:PRK11300 243 NNP 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-242 |
1.48e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNT--------- 87
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVadknqlrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 ------VFQSYALFPHMSVFENVAFG----LRMQKTPAAEitpRVLDALRMVQLEEFAQRK-PHQLSGGQQQRVAIARAV 156
Cdd:PRK10619 91 rtrltmVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 157 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*.
gi 490998897 237 FVASFI 242
Cdd:PRK10619 247 RLQQFL 252
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-229 |
5.35e-35 |
|
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: 134.88 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmSV 100
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVAfglRMqktpaAEITP-RVLDALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG4618 423 AENIA---RF-----GDADPeKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 169 LSALDYKLRKQMQNELKALqRKLGITFVFVTHDQeEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-220 |
6.29e-35 |
|
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: 126.18 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmSVFEN 103
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VafglrmqktpaaeitprvldalrmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 490998897 184 LKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGKI 220
Cdd:cd03246 139 IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-229 |
1.07e-34 |
|
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: 134.07 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmS 99
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlRMQKTPAAEItprvLDALRMVQLEEFAQRKP---HQ--------LSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:TIGR02203 422 IANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 169 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-234 |
1.20e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.08 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 33 TINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH-----VNTVFQS-YA-LFPHMSVFENVA 105
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkIQIVFQNpYGsLNPRKKVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 106 FGLRMQKT-PAAEITPRVLDALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:PRK11308 117 EPLLINTSlSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490998897 184 LKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-233 |
1.37e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 128.57 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSF-DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRI---HLEDQDITHVPAENRHVN 86
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQS-YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-235 |
2.21e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 127.34 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL-----ENVDSGRIHLEDQDITHVPAE--NRH 84
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYALFPHMSVFENVAFGLRMQK--TPAAEITPRVLDALRMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVN 158
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 159 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 235
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-228 |
5.40e-34 |
|
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: 125.42 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFD-GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFP 96
Cdd:cd03254 11 SYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 HmSVFENVAFGlrmqkTPAAEITpRVLDALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:cd03254 91 G-TIMENIRLG-----RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-237 |
5.43e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 131.75 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLSPLVQLAGIRKSF-----------DGKTVISDLNLTINNGEFLTLLGPSGCGKTT----VLRLIAGlenvdSGRIH 69
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 70 LEDQDITH------VPAENRhVNTVFQ--SYALFPHMSVFENVAFGLRM-QKT-PAAEITPRVLDALRMVQLE-EFAQRK 138
Cdd:PRK15134 344 FDGQPLHNlnrrqlLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 139 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 218
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250
....*....|....*....
gi 490998897 219 KIEQDGTPREIYEEPKNLF 237
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEY 521
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-232 |
1.75e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT-HVPAE--NRHVN 86
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaiALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFGLRmqKTPAAEITPRVLDAlrmvQLEEFAQR---------KPHQLSGGQQQRVAIARAVV 157
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLE--PTKGGRLDRKAARA----RIRELSERygldvdpdaKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 158 NKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG3845 158 RGARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-236 |
3.37e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.82 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAEN-----RHVNTVFQSY-ALFPHMSV 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENvwnlrRKIGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 180
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 181 QNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-229 |
4.55e-33 |
|
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: 130.25 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAE-NRHVNTVFQSYALFPHmS 99
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlrmqkTPAAEITpRVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:TIGR01846 547 IRDNIALC-----NPGAPFE-HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 169 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-229 |
4.83e-33 |
|
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: 123.37 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE--NRHVNTVFQSYALFpHMS 99
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGlrmqkTPAAEITpRVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:cd03252 92 IRDNIALA-----DPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 169 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-200 |
7.26e-33 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 128.77 E-value: 7.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvPAENRhvnTVF---QSYalFPHM 98
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpqRPY--LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFGLRMQKTPAAEItprvLDALRMVQLEEFAQR------KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:COG4178 441 TLREALLYPATAEAFSDAEL----REALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*....
gi 490998897 173 DYKLRKQMqneLKALQRKL-GITFVFVTH 200
Cdd:COG4178 517 DEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-232 |
1.19e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 122.81 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS---------GR-IHLEDQDITH 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRtVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 78 VPAENRHVNTVFQSYALFPHMSVFENVAFGlRMQKTP---------AAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQ 148
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 149 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 490998897 229 IYEE 232
Cdd:PRK09984 240 FDNE 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-204 |
1.85e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 121.36 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE--NRHVN 86
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHmSVFENVAFGLRM-QKTPAAEitpRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIrNQQPDPA---IFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 204
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-235 |
2.72e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.87 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD-----------SGR-IHLEDQDITHVpaeNRHVNTVFQSYA 93
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvegevrlFGRnIYSPDVDPIEV---RREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 94 LFPHMSVFENVAFGLRMQK--TPAAEITPRVLDALRMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 168 SLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 235
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-220 |
4.22e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.36 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT-----HVPAENRHVNTVFQSYALFPH 97
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 178 KQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK10908 174 EGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-232 |
4.36e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.88 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH----VPAENRHVNTVFQS--YALF 95
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PhMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:PRK13636 97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 176 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-228 |
4.48e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.15 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSF---DGKT-VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-- 81
Cdd:PRK10535 1 MTALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 ----NRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 157
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 158 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-232 |
5.34e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVntvfqsyALFP--HM- 98
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRL-------ALLPqhHLt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 ----SVFENVAFGlrmqKTP--------AAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:PRK11231 88 pegiTVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 167 ESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK11231 164 EPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
6.70e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.12 E-value: 6.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFDGKT-----VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH--LEDQDITHVPAEN------- 82
Cdd:PRK13651 8 IVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 -----------------RHVNTVFQ--SYALFpHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQL 142
Cdd:PRK13651 88 viqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 143 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQ 222
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
250
....*....|....
gi 490998897 223 DGTPREIYEEPKNL 236
Cdd:PRK13651 246 DGDTYDILSDNKFL 259
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-232 |
6.97e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.39 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 21 FDGKTvISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH------VPAENRHVNTVFQsyal 94
Cdd:PRK13649 18 FEGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 95 FPHMSVFE-----NVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:PRK13649 93 FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 169 LSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-223 |
1.81e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 118.73 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 25 TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR------HVNTVFQSYALFPHM 98
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 178
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490998897 179 QMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGKIEQD 223
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-229 |
2.42e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 122.64 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE--NRHVNT 87
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENVafglRMQKTP-------AAEITPRVLD-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 159
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVV----EMGRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 160 PRLLLLDESLSALDykLRKQMQNelKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-215 |
2.62e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 124.32 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKT-VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHV 85
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHmSVFENVAFGLRMQktPAAEITprvlDALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIAR 154
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDA--SDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMsDRIVVM 215
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-233 |
6.74e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.22 E-value: 6.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS-----GRIHLEDQDI----THV 78
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 79 PAENRHVNTVFQSYALFPhMSVFENVAFGLRMQK-TPAAEITPRVLDALRMVQLEEFAQRKPHQ----LSGGQQQRVAIA 153
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-----RDGKIEQDGTPRE 228
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKK 242
|
....*
gi 490998897 229 IYEEP 233
Cdd:PRK14258 243 IFNSP 247
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-167 |
1.14e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 117.14 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSlSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPa 80
Cdd:COG4674 1 MSLDTMH-GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ENRHVNT----VFQSYALFPHMSVFENVAFGLRMQKTP--------AAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQ 148
Cdd:COG4674 79 EHEIARLgigrKFQKPTVFEELTVFENLELALKGDRGVfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
170
....*....|....*....
gi 490998897 149 RVAIARAVVNKPRLLLLDE 167
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDE 177
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
1.47e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.53 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENRH-----VNTVFQSY--AL 94
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKwvrskVGLVFQDPddQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 95 FPhMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:PRK13647 93 FS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 175 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPR 227
Cdd:PRK13647 172 RGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-228 |
2.31e-30 |
|
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: 121.85 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFpHMSVFENVAF 106
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 GlRMQKTPAAeitprVLDALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 175
Cdd:COG5265 455 G-RPDASEEE-----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 176 LRKQMQNELKALQRklGITFVFVTH------DqeealtmSDRIVVMRDGKIEQDGTPRE 228
Cdd:COG5265 529 TERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-259 |
2.71e-30 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 118.29 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSF---DGK-TVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL---ENVDSGRIHLEDQDITHVPAE 81
Cdd:PRK09473 10 DALLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 --NR----HVNTVFQS--YALFPHMSVFENVAFGL----RMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQR 149
Cdd:PRK09473 90 elNKlraeQISMIFQDpmTSLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
250 260 270
....*....|....*....|....*....|
gi 490998897 230 YEEPKNLFvasfigEINLFNAtvIERLDEQ 259
Cdd:PRK09473 250 FYQPSHPY------SIGLLNA--VPRLDAE 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-235 |
2.81e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.89 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-----RHVNTVFQS-YA-LFPHMSVFENVAFGLR 109
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 110 MQKT-PAAEITPRVLDALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKAL 187
Cdd:PRK10261 430 VHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 188 QRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 235
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-229 |
5.60e-30 |
|
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: 120.53 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmSVF 101
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAfglRMQKTPAAEitpRVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:TIGR01842 410 ENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 171 ALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-233 |
6.59e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.98 E-value: 6.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT---HVpAENRHVNTVFQSYALFPHmSVFE 102
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHH-YLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGLRmqKTPAAEITprvlDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:TIGR00958 574 NIAYGLT--DTPDEEIM----AAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 172 LDyklrKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:TIGR00958 648 LD----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-235 |
7.26e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.26 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVD-----SGRIHLEDQDI----THVP 79
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 80 AENRHVNTVFQSYALFPhMSVFENVAFGLRMQKTPAAEITPRVLD-ALRMVQLEEFAQRKPHQ----LSGGQQQRVAIAR 154
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 490998897 235 N 235
Cdd:PRK14239 240 H 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-232 |
9.35e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.52 E-value: 9.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGktvisdLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSG----RIHLEDQDITHVPAENR-----HVN 86
Cdd:TIGR03269 295 GVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGRgrakrYIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENV--AFGLRMQKTPAAEitpRVLDALRMV-----QLEEFAQRKPHQLSGGQQQRVAIARAVVNK 159
Cdd:TIGR03269 369 ILHQEYDLYPHRTVLDNLteAIGLELPDELARM---KAVITLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 160 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-246 |
1.77e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ------DITHVPA--ENRHVNTVFQSYA 93
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 94 LFPHMSVFENVAFGLRMQKTPAA-EITPRVLDALRMVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 169 LSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASF-IGEIN 246
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRIS 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-220 |
4.03e-29 |
|
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: 110.98 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRksfdGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT------------- 76
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdairagia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 77 HVPaENRHvntvfqSYALFPHMSVFENVAFglrmqktpaaeitprvldalrmvqleefaqrkPHQLSGGQQQRVAIARAV 156
Cdd:cd03215 79 YVP-EDRK------REGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 157 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-200 |
5.50e-29 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 111.43 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRksfDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR-------H 84
Cdd:PRK13538 5 RNLACER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllylgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNtvfqsyALFPHMSVFENVAFGLRMQKTPAAEitpRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK13538 82 QP------GIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLGITfVFVTH 200
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
1.44e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 116.30 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA 80
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ENRH---VNTVFQSYALFPHMSVFENVAFGLrmqktPAAEITPRVLDALrMVQLEefAQRKPHQLSG----GQQQRVAIA 153
Cdd:PRK15439 81 AKAHqlgIYLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL-LAALG--CQLDLDSSAGslevADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-230 |
2.68e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED-------QDITHVPAENRHVNTVFQsyalFPHMS 99
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQ----FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFE-----NVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:PRK13645 103 LFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 174 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 230
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-236 |
3.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.46 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT------HVPAENRHVNTVFQsyalFPHMSV 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FEN-----VAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:PRK13641 99 FENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 175 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-233 |
4.75e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 4.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT--HVPAENRHVNTVFQSyalfPHMSVF 101
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQN----PDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 -----ENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK13652 93 sptveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 177 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-224 |
5.88e-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: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLeDQDITHVPAenrhVNTVFQsyalfPHMSVFEN 103
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLLG----LGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490998897 184 LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03220 185 LRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-232 |
6.09e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 18 RKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH--------LEdqdithvpaenrhVNTVF 89
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsalLE-------------LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QsyalfPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:COG1134 100 H-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 170 SALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:COG1134 175 AVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-229 |
6.80e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.60 E-value: 6.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 19 KSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH---VNTVFQSYALF 95
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PHMSVFENVAFGLRMQKTPAAEI-TPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 175 KLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK10895 171 ISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-229 |
1.23e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 109.69 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHMSVF 101
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGlRMQKTPA-----AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK10253 100 ELVARG-RYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 177 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-218 |
1.38e-27 |
|
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: 108.29 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSF-----DGKT--VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ----DITH 77
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 78 vpAENRHV-----NT---VFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQ 148
Cdd:COG4778 82 --ASPREIlalrrRTigyVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 149 RVAIARAVVNKPRLLLLDESLSALDYKLR---KQMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDG 218
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-240 |
2.05e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.86 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP------AENR 83
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HvntVFQSYALFPHmsvfENVAFGLRMQKTPAAEITPRV---------------LDALRMVQLEefAQR---KPHQLSGG 145
Cdd:PRK11701 85 R---LLRTEWGFVH----QHPRDGLRMQVSAGGNIGERLmavgarhygdirataGDWLERVEID--AARiddLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 146 QQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IEQDG 224
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRvVESGL 235
|
250 260
....*....|....*....|..
gi 490998897 225 T------PREIYEEpknLFVAS 240
Cdd:PRK11701 236 TdqvlddPQHPYTQ---LLVSS 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-201 |
2.22e-27 |
|
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: 112.84 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDG-KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA-ENRHVNT 87
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VF-QSYALFpHMSVFENVAFGlRMQKTPAAeitprVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 155
Cdd:TIGR02868 413 VCaQDAHLF-DTTVRENLRLA-RPDATDEE-----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490998897 156 VVNKPRLLLLDESLSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHD 201
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLlAALSGR---TVVLITHH 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-231 |
4.49e-27 |
|
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: 112.20 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV--DSGRI--------------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 69 -------HLEDQDI-------THVPAENRHVNTVFQ-SYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEE 133
Cdd:TIGR03269 81 pcpvcggTLEPEEVdfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 134 FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 213
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 490998897 214 VMRDGKIEQDGTPREIYE 231
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-236 |
4.91e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 4.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHvPAENRHVNTVFQSYAL---FPHMSVFEN 103
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYIRPVRKRIGMvfqFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 -----VAFGLRMQKTPAAEITPRVLDALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:PRK13646 102 tvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 178 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNL 236
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-244 |
7.79e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 107.18 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR--HVNTVFQ--SYALFPHMSVFE 102
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsqRIRMIFQdpSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGLRMQ-KTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 180
Cdd:PRK15112 109 ILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 181 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP-----KNLfVASFIGE 244
Cdd:PRK15112 189 INLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlheltKRL-IAGHFGE 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-298 |
8.14e-27 |
|
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: 111.07 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVDSGRIHLEDQDI--THV-PAENRHV 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIrDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFG----LRMQKTPAAEITPRVLDALRMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKP 160
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 161 RLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGkieqdgtpREIYEEPknlfvas 240
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--------QHVATKD------- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 241 figeinlfnatvIERLDEQRVRASVEGREC-NIYVNFPVERGqrlNVLLRPEDL-----------RVDEV 298
Cdd:TIGR02633 225 ------------MSTMSEDDIITMMVGREItSLYPHEPHEIG---DVILEARNLtcwdvinphrkRVDDV 279
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-230 |
1.15e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.02 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 21 FDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH----VPAENRHVNTVFQSyalfP 96
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 HMSVF-----ENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:PRK13638 87 EQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 172 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 230
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-215 |
1.20e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvpAENRHVNTVFQSYAL---FP 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR---------AGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 hMSVFENVAFGL----RMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 173 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTmSDRIVVM 215
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-242 |
2.71e-26 |
|
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: 110.60 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP--AENRHVNTVFQSYALFPHmSV 100
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENvafgLRMQKTPAAEITpRVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:TIGR01193 565 LEN----LLLGAKENVSQD-EIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 170 SALDYKLRKQMQNELKALQRKlgiTFVFVTHDQEEAlTMSDRIVVMRDGKIEQDGTPREIYEEpkNLFVASFI 242
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-246 |
2.89e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.95 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ--------DITHVPA 80
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ENRHVNTVFQSYALFPhMSVFENVAFGLRMQK-TPAAEITPRVLDALRMVQLEEFAQRK----PHQLSGGQQQRVAIARA 155
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 156 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKN 235
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
250
....*....|.
gi 490998897 236 LFVASFIGEIN 246
Cdd:PRK14271 256 AETARYVAGLS 266
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-173 |
3.90e-26 |
|
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: 103.59 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE-NRHVNTVFQSYALFPHMSV 100
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 101 FENVAFGLRMQKTPAAEItprvLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-232 |
6.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.20 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 29 DLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN------RHVNTVFQsyalFPHMSVFE 102
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQ----FPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 -----NVAFGLRMQKTPAAEITPRVLDALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK13643 100 etvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 177 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK13643 180 RIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-225 |
1.16e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.87 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKT----TVLRLIAGLENV-DSGRIHLEDQDITHVPAEN-RHVN--- 86
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTlRGVRgnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 --TVFQS--YALFPHMSV----FENVAFGLRMQKTPA-AEItprvLDALRMVQLEEFAQR---KPHQLSGGQQQRVAIAR 154
Cdd:PRK15134 94 iaMIFQEpmVSLNPLHTLekqlYEVLSLHRGMRREAArGEI----LNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IEQDGT 225
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQNRA 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-219 |
1.67e-25 |
|
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: 102.16 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 19 KSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQdITHVPAENRHVNTvfqsyalfphm 98
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVSQEPWIQNG----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFGLRMQKtpaaeitPRVLDALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03250 81 TIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 168 SLSALDYKLRKQ-MQNELKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGK 219
Cdd:cd03250 154 PLSAVDAHVGRHiFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-200 |
1.75e-25 |
|
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: 100.69 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-EDQDITHVPAEnrhvntvfqsyalfPHMSV 100
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQR--------------PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 fenvafG-LRmqktpaaeitprvlDALRmvqleefaqrKP--HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDyklr 177
Cdd:cd03223 78 ------GtLR--------------EQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD---- 123
|
170 180
....*....|....*....|...
gi 490998897 178 KQMQNELKALQRKLGITFVFVTH 200
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-221 |
1.88e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDqdithvpaenrh 84
Cdd:COG0488 309 ERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 vnTVFQSY------ALFPHMSVFENVAFGLRMQKtpaaEITPRVLdalrmvqLEEF-----AQRKP-HQLSGGQQQRVAI 152
Cdd:COG0488 377 --TVKIGYfdqhqeELDPDKTVLDELRDGAPGGT----EQEVRGY-------LGRFlfsgdDAFKPvGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 153 ARAVVNKPRLLLLDE--------SLSALdyklrkqmqneLKALQRKLGiTFVFVTHDQE--EALTmsDRIVVMRDGKIE 221
Cdd:COG0488 444 AKLLLSPPNVLLLDEptnhldieTLEAL-----------EEALDDFPG-TVLLVSHDRYflDRVA--TRILEFEDGGVR 508
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-237 |
2.49e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.24 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL----ENVDSGRIHLEDQDITHVpaeNRHVNTVFQSYALF 95
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyqGSLKINGIELRELDPESW---RKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 pHMSVFENVAFGlrmqktpAAEITP-RVLDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLL 163
Cdd:PRK11174 436 -HGTLRDNVLLG-------NPDASDeQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 164 LLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPkNLF 237
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-173 |
2.57e-25 |
|
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: 101.42 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRksfDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHV-PAENRHVNTVFQ 90
Cdd:cd03231 4 DELTCER---DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAaeitprVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 490998897 171 ALD 173
Cdd:cd03231 155 ALD 157
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-173 |
8.35e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 8.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 14 LAGIRKsfdGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH-VPAENRHvntvfqsY 92
Cdd:PRK13539 8 LACVRG---GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACH-------Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 -----ALFPHMSVFENVAFGLRMQKTPAAEITprvlDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:PRK13539 78 lghrnAMKPALTVAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*.
gi 490998897 168 SLSALD 173
Cdd:PRK13539 154 PTAALD 159
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-225 |
9.15e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.81 E-value: 9.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 2 NIQPRSLSPLVQLAGIRKSFDGKT-VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPA 80
Cdd:PRK13657 325 AIDLGRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 EN--RHVNTVFQSYALFpHMSVFENvafgLRMQKTPAAEitPRVLDALRMVQLEEFAQRKPH-----------QLSGGQQ 147
Cdd:PRK13657 405 ASlrRNIAVVFQDAGLF-NRSIEDN----IRVGRPDATD--EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 148 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVfVTHdQEEALTMSDRIVVMRDGKIEQDGT 225
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-219 |
1.22e-24 |
|
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: 97.90 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGrihledqdithvpaenrhvntvfqs 91
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 yalfphmsvfenvafglrmqktpaaeiTPRVLDALRMVQLEefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03221 56 ---------------------------IVTWGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 172 LDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-225 |
1.38e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.91 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 4 QPRSLSPLVQLAGIRKSFDGKT--VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAE 81
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 N--RHVNTVFQSYALFPHmSVFENvafgLRMQKTPAAEitPRVLDALRMVQLEEFAQRKP----------HQLSGGQQQR 149
Cdd:PRK11160 411 AlrQAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDGT 225
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQiLELLAEHAQNK---TVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-219 |
2.65e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS--GRIHLEDQDIT--HV-PAENR 83
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQasNIrDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 HVNTVFQSYALFPHMSVFENVAFGlrmqktpaAEITP-----------RVLDALRMVQLEEFAQRKPHQLSGGQQQRVAI 152
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLG--------NEITPggimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 153 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-241 |
3.18e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 99.80 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQ-DITHVPaenrhvn 86
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 tvfQSYALFPHMSVfeNVAFGLRMQK-TPAAEITPrvldALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:PRK09544 74 ---QKLYLDTTLPL--TVNRFLRLRPgTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMrDGKIEQDGTPREIYEEPKnlFVASF 241
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-220 |
6.80e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 97.24 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENV--DSGRIHLEDQDItHVPAENRHVNTVFQSYALFPHMSV 100
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVAFglrmqktpAAEitprvldaLRmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 180
Cdd:cd03213 100 RETLMF--------AAK--------LR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490998897 181 QNELKALqRKLGITFVFVTHD-QEEALTMSDRIVVMRDGKI 220
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-245 |
1.07e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKT-TVLRLIAGLE----NVDSGRIHLEDQD------ITHVPAENRHVN-----TVFQ 90
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEqaggLVQCDKMLLRRRSrqvielSEQSAAQMRHVRgadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 S--YALFPHMSVFENVAFGLRMQ----KTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHqgasREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLFVASFIGE 244
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
.
gi 490998897 245 I 245
Cdd:PRK10261 272 V 272
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-229 |
1.10e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.71 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT--HV 78
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 79 PAENRHVNTVFQSYALFPHMSVFENVAFGlrmqKTP--------AAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRV 150
Cdd:PRK10575 81 KAFARKVAYLPQQLPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 151 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-220 |
1.14e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 97.54 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRH--VNTVFQSYALFPHmSVFEN 103
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHskVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGLR---MQKTPAAEITPRVLDALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 178
Cdd:cd03248 108 IAYGLQscsFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490998897 179 QMQnelKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03248 188 QVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-224 |
1.64e-23 |
|
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: 97.40 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 18 RKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDqditHVPAENR-----HVNTVF-QS 91
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRkkflrRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490998897 172 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-236 |
2.14e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.60 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENvDSGRIHLEDQDITHVPA-ENRHVNTVF--QSYALFPhMSVFENVAF 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaELARHRAYLsqQQSPPFA-MPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 GLRmQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV------VN-KPRLLLLDESLSALDYklrkQ 179
Cdd:COG4138 93 HQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV----A 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 180 MQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYeEPKNL 236
Cdd:COG4138 168 QQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-220 |
3.11e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN---RHVNTVFQSYALFPHMSVFE 102
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAF-GLRMQKTPAAEITPRVLDALRMVQlEEFAQRKpHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 181
Cdd:PRK11614 100 NLAMgGFFAERDQFQERIKWVYELFPRLH-ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 490998897 182 NELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK11614 178 DTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-210 |
5.37e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.77 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLEnVDsGRIHLEDQDI--THV-PAE-NRHVNTVFQSYALF 95
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR-VE-GKVTFHGKNLyaPDVdPVEvRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PHmSVFENVAFGLRMQ--KTPAAEITPRvldALRMVQLEEFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:PRK14243 104 PK-SIYDNIAYGARINgyKGDMDELVER---SLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490998897 170 SALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSD 210
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-220 |
5.88e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIR-KSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT------------ 76
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglsprerrrlgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 77 -HVPaENRHvntvfqSYALFPHMSVFENVAFGLRMQKtpaaEITPRVLdaLRMVQLEEFAQRK----------PHQ---- 141
Cdd:COG3845 336 aYIP-EDRL------GRGLVPDMSVAENLILGRYRRP----PFSRGGF--LDRKAIRAFAEELieefdvrtpgPDTpars 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 142 LSGGQQQRVAIARAVVNKPRLLL-------LDESLSAldyklrkQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVV 214
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIaaqptrgLDVGAIE-------FIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAV 474
|
....*.
gi 490998897 215 MRDGKI 220
Cdd:COG3845 475 MYEGRI 480
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-220 |
6.11e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH-------------VPaENRHvntvf 89
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVP-EDRK----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 qSYALFPHMSVFENVAFGLRMQKTPAaeitpRVLDALRMVQL-EEFAQR---KPH-------QLSGGQQQRVAIARAVVN 158
Cdd:COG1129 338 -GEGLVLDLSIRENITLASLDRLSRG-----GLLDRRRERALaEEYIKRlriKTPspeqpvgNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 159 KPRLLLLDESLSALD-------YKLrkqMqNELKAlqRKLGItfVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakaeiYRL---I-RELAA--EGKAV--IVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-220 |
1.69e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.26 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVD--SGRIHLEDQDIThvPAE-NRHVNTVFQSYALFPHMSVF 101
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGttSGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFG--LRMQ-KTPAAEITPRVLD-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:cd03234 100 ETLTYTaiLRLPrKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 178 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
33-234 |
1.74e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.73 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 33 TINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDQDITHVPAENRH------VNTVFQS--YALFPHMSV 100
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVAFGLRM-QKTPAAEITPRVLDALRMVQLEEFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:PRK11022 109 GFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 177 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:PRK11022 189 QAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-173 |
2.16e-22 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 93.76 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVpA 80
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 81 ENRHVNTVFQSYALFPHMSVFENVAF-----GLRMQKTPAaeitprvlDALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 155
Cdd:PRK13543 80 RSRFMAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMPG--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARL 151
|
170
....*....|....*...
gi 490998897 156 VVNKPRLLLLDESLSALD 173
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
2.65e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 1 MNIQPRSLSPLVQLAGIRKSFDGKT-----VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED--- 72
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 73 -QDITHVPAENRH--------------VNTVFQ--SYALFPHmSVFENVAFG---LRMQKTPAAEITPRVLDalRMVQLE 132
Cdd:PRK13631 91 gDKKNNHELITNPyskkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--KMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 133 EFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQnELKALQRKLGITFVFVTHDQEEALTMSDRI 212
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|.
gi 490998897 213 VVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-232 |
3.31e-22 |
|
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: 92.98 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDQDITHVPAENRHVNTVFqsyalfphms 99
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 vfenvafgLRMQKTPaaEITP-RVLDALRMVQlEEFaqrkphqlSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 178
Cdd:cd03217 81 --------LAFQYPP--EIPGvKNADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 179 QMQNELKALqRKLGITFVFVTHDQEEALTM-SDRIVVMRDGKIEQDGtPREIYEE 232
Cdd:cd03217 142 LVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-220 |
5.90e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 14 LAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE-DQDITHVPaenrhvntvfQSY 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENVAFGLR------------MQKTPAAEITPRVLDAL--RMVQL-------------------EEFAQRKP 139
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELqeEFEALggweaearaeeilsglgfpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 140 HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklgITFVFVTHDQE--EALTmsDRIVVMRD 217
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHDRYflDRVA--TRILELDR 224
|
...
gi 490998897 218 GKI 220
Cdd:COG0488 225 GKL 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-226 |
7.48e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDQDITHVPAENRH---VNTVFQSYAL 94
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAragIFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 95 FPHMSV--FENVAFGLRMQKT-PAAEITPRVLDALRMVQL-EEFAQRKPHQ-LSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:COG0396 89 IPGVSVsnFLRTALNARRGEElSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 170 SALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTM--SDRIVVMRDGKIEQDGTP 226
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-224 |
3.09e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 89.68 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRHVNTVF-QSYALFpHMSVFE 102
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLnQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVafGLRmqktpaaeitprvldalrmvqleefaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 182
Cdd:cd03247 94 NL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998897 183 EL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:cd03247 140 LIfEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-226 |
3.36e-21 |
|
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: 90.63 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTV----LRLIagleNVDSGRIHLEDQDITHVPaenrhVNTVFQSYALFPH 97
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIG-----LHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 msvfENVAFG--LRMQKTPAAEITP-RVLDALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLL 163
Cdd:cd03244 86 ----DPVLFSgtIRSNLDPFGEYSDeELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 164 LLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTP 226
Cdd:cd03244 162 VLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-233 |
7.87e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.01 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmSVF 101
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGlRMQKTP-----AAEITPRVLDALRMVQ--LEEFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:PRK10789 407 NNIALG-RPDATQqeiehVARLASVHDDILRLPQgyDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 175 KLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK10789 485 RTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-284 |
8.95e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQD---ITHVPAENRHVN 86
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQSYALFPHMSVFENVAFG--------------LRMQKTPAAEITPRVldALRmVQLEEFAQrkphQLSGGQQQRVAI 152
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrhltkkvcgvniidWREMRVRAAMMLLRV--GLK-VDLDEKVA----NLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 153 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG-----KIEQDGTPR 227
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSND 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 228 EIY-----EEPKNLFVASFIGEINLFNATVIE-----RLDEQRVRAsvegrecniyVNFPVERGQRL 284
Cdd:PRK09700 236 DIVrlmvgRELQNRFNAMKENVSNLAHETVFEvrnvtSRDRKKVRD----------ISFSVCRGEIL 292
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-226 |
3.26e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 92.77 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 8 LSPLVQLAGIRKSFD--GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI-THVPAENRH 84
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 165 LDESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTP 226
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-232 |
7.67e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTV--ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALF 95
Cdd:PRK11176 350 TYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 pHMSVFENVAFGlRMQKTPAAEITprvlDALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK11176 430 -NDTIANNIAYA-RTEQYSREQIE----EAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-269 |
7.88e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDqditHVPAENRHVN-----TVF-QSYALFPH 97
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKEFarrigVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENvaFGL--RMQKTPAAEITPRvLDALR-MVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:COG4586 111 LPAIDS--FRLlkAIYRIPDAEYKKR-LDELVeLLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 175 KLRKQMQNELKALQRKLGITFVFVTHDQE--EALtmSDRIVVMRDGKIEQDGTP---REIYEEPKNLFV--ASFIGEINL 247
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLeelKERFGPYKTIVLelAEPVPPLEL 265
|
250 260
....*....|....*....|..
gi 490998897 248 FNATVIERLDEQRVRASVEGRE 269
Cdd:COG4586 266 PRGGEVIEREGNRVRLEVDPRE 287
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-203 |
1.33e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.17 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--NVDSGRIHLEDQDIThvpaenrhvntvfq 90
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 syalfPHMSVFENVAfglRMQKTPAAeitprvLDALRMVQLEE--FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG2401 98 -----REASLIDAIG---RKGDFKDA------VELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....*
gi 490998897 169 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQE 203
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-229 |
2.05e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 86.80 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG--LENVDS------GRIHLEDQDITHVPAEN---RHVNTVFQ 90
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAAIDAPRlarLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPhMSVFENVAFGLRMQKTPAAEITPRVLD----ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN-------- 158
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 159 -KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-228 |
3.59e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.88 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENR-----HVNTVFQSYALFPHMSVFENv 104
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPedyrkLFSAVFTDFHLFDQLLGPEG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 105 afglrmqKTPAAEITPRVLDALRM---VQLEEFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 181
Cdd:PRK10522 418 -------KPANPALVEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 182 NELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGKI-EQDGTPRE 228
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERD 536
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-326 |
4.24e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.52 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT-HVPAENRH--V 85
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFGlRMQKTPAAEITPRVLDA-----LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 160
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMYAeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 161 RLLLLDESLSAL-DYKLRK--QMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGKIeqdgtpreIYEEPknlf 237
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESlfRVIRELKSQGR--GI--VYISHRLKEIFEICDDVTVFRDGQF--------IAERE---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 238 VASfIGEINLFNATVIERLDEQRVRASVEGRECNIYVN-----------FPVERGQRLNV--LL---RPEDLRV------ 295
Cdd:PRK10762 225 VAD-LTEDSLIEMMVGRKLEDQYPRLDKAPGEVRLKVDnlsgpgvndvsFTLRKGEILGVsgLMgagRTELMKVlygalp 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490998897 296 ----------DEVHDGSDADGL---IGYIRE-RNYKGMTLE-SVVE 326
Cdd:PRK10762 304 rtsgyvtldgHEVVTRSPQDGLangIVYISEdRKRDGLVLGmSVKE 349
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-220 |
7.59e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.75 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI-THVPAENRHVNTVFQSY-----ALFPHMSV 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVA------FGLRMQKTPAAEITPRVLDALRMvqleeFAQRKPHQ------LSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 169 LSALDYKLRK---QMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK10762 423 TRGVDVGAKKeiyQLINQFKA----EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-234 |
9.54e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.75 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTViSDLNLTINNGEFLTLLGPSGCGKT-TVLRLI----AGLENVdSGRIHLEDQDITHVPAENRHVN 86
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQT-AGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 87 TVFQS--YALFPHMSVFENVAFGLRMQKTPAAEitPRVLDALRMVQLEE---FAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPK 234
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-233 |
9.56e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.60 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLeNVDSGRIHLEDQDITHVPA-ENRHVNTVF--QSYALFpHMSVFENVAF 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaELARHRAYLsqQQTPPF-AMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 GLRmQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIArAVV------NKP--RLLLLDESLSALDYKLRK 178
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 179 QMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEP 233
Cdd:PRK03695 171 ALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-233 |
1.57e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.34 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISD-LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDQDITHVPAENRH------VNTVFQ 90
Cdd:COG4170 17 QGRVKAVDrVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRkiigreIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 --SYALFPHMSVFENVafglrMQKTPAAEITPRVLDalrmvqleEFAQRK----------------------PHQLSGGQ 146
Cdd:COG4170 97 epSSCLDPSAKIGDQL-----IEAIPSWTFKGKWWQ--------RFKWRKkraiellhrvgikdhkdimnsyPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 147 QQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTP 226
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
....*..
gi 490998897 227 REIYEEP 233
Cdd:COG4170 244 EQILKSP 250
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-218 |
1.57e-18 |
|
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: 83.15 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN-RHVNTVFQSYA----LFPH 97
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtRSRNRYSVAYAaqkpWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVAFGLRMQK------TPAAEITPRVlDALRMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03290 93 ATVEENITFGSPFNKqrykavTDACSLQPDI-DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 172 LDYKLRKQMQNE--LKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDG 218
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-232 |
4.37e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP--AENRHVNTVFQSYALFPHmS 99
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 VFENVAFGLRMQKTpaaeitpRVLDALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:PRK10790 431 FLANVTLGRDISEE-------QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 169 LSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-220 |
9.06e-18 |
|
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: 80.77 E-value: 9.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVD-SGRIHL--EDQDITHVPAEnRHVNTVFQS 91
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYngIPYKEFAEKYP-GEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 YALFPHMSVFENVAFGLRMQktpaaeitprvldALRMVqleefaqRKphqLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCK-------------GNEFV-------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490998897 172 LDYKLRKQMQNELKALQRKLGIT-FVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-232 |
9.31e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.79 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 3 IQPRSLSPLVQLA----GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-----EDQ 73
Cdd:NF033858 254 IPPRPADDDDEPAiearGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 74 DIthvpAENRHVNTVFQSYALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIA 153
Cdd:NF033858 334 DI----ATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFV-THDQEEALTmSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-219 |
1.38e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI---THVPAENRHV 85
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 86 NTVFQSYALFPHMSVFENVAFGLRMQKtpAAEITPRVLDALRMVQLEEFA-----QRKPHQLSGGQQQRVAIARAVVNKP 160
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHK--GGIVNRRLLNYEAREQLEHLGvdidpDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 161 RLLLLDE---SLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:PRK11288 160 RVIAFDEptsSLSAREIEQLFRVIRELRAEGRVI----LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-232 |
3.55e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.25 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFdGKTV-ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIthvpAENRHVNTVFQ 90
Cdd:NF033858 2 ARLEGVSHRY-GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYA---------LFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 162 LLLLDESLSALDYKLRKQ---MQNELKAlqRKLGITFVFVTHDQEEALTMsDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-224 |
8.37e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.13 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEdQDITHVPAENRHVNTVFQSYALFphmsvFEN 103
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAWIMNATVRGNILF-----FDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 vafglrmqktpaaEITPRVLDALRMVQLE-EFAQ----------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:PTZ00243 747 -------------EDAARLADAVRVSQLEaDLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490998897 173 DYKLRKQMQNELkALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDG 224
Cdd:PTZ00243 814 DAHVGERVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-210 |
1.13e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.68 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 17 IRKSFD--GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH-VPAENRHVNTVFQSYA 93
Cdd:PRK13540 5 IELDFDyhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 94 LFPHMSVFENVAFGLRMQKTpAAEITprvlDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPG-AVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 490998897 174 YKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSD 210
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-220 |
2.06e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 28 SDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENR-HVNTVF-----QSYALFPHMSVF 101
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVA------FGLRMQKTPAAEITPRVLDAL--RMVQLEEFAQRkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:PRK15439 360 WNVCalthnrRGFWIKPARENAVLERYRRALniKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490998897 174 YKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK15439 436 VSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
64-229 |
2.20e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 64 DSGRIHLEDQDITHVPAEN-RHVNTVFQSYALFPHMSVFENVAFGlrmQKTPAAEITPRvldALRMVQLEEFAQRKPHQ- 141
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG---KEDATREDVKR---ACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 142 ----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSDR 211
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|...
gi 490998897 212 IVVM----RDGK-IEQDGTPREI 229
Cdd:PTZ00265 1428 IVVFnnpdRTGSfVQAHGTHEEL 1450
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-226 |
4.62e-16 |
|
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: 75.91 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFphmsvfen 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLF-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 vAFGLRMQKTPAAEITPR-VLDALRMVQLEEfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY----KLRK 178
Cdd:cd03369 95 -SGTIRSNLDPFDEYSDEeIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYatdaLIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 179 QMQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTP 226
Cdd:cd03369 167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-201 |
9.02e-16 |
|
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: 78.44 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvpAENRHVNTVFQS 91
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 Y-ALFPHMSVFENVAFGLRMQKTPAAEITPRVLdalrmvqLEEFA------QRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRAY-------VGRFNfkgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490998897 165 LDESLSALDYklrkqmqNELKALQRKL----GITFVfVTHD 201
Cdd:TIGR03719 467 LDEPTNDLDV-------ETLRALEEALlnfaGCAVV-ISHD 499
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-221 |
1.02e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.29 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDS--GRIHLEDQ-----DITHvpAENRHVNTV 88
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD--SEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFGLRMQKTPA---AEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 166 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGK-IE 221
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-219 |
1.67e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 19 KSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL--ENVDSGRIHLEDQDITHVPAenRHVNTVFQSYALFP 96
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQIL--KRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 HMSVFENVAFG--LRMQKTPAAEITPRVLDALrmvqLEEFAQRKPHQ----------LSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PLN03211 154 HLTVRETLVFCslLRLPKSLTKQEKILVAESV----ISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGK 219
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-200 |
2.60e-15 |
|
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: 77.48 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHL-EDQDITHVPAENRHVNTVFQSYALFPhMSVF 101
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpAKGKLFYVPQRPYMTLGTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGLRMQktpaaeitprVLDA-LRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:TIGR00954 543 DMKRRGLSDK----------DLEQiLDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 490998897 172 LDYKLRKQMQNelkaLQRKLGITFVFVTH 200
Cdd:TIGR00954 613 VSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-225 |
4.66e-15 |
|
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: 76.98 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKT--VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpaenRHVNTV 88
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFG-------LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPR 161
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998897 162 LLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGT 225
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-229 |
4.72e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLR-LIAGLENVDsGRIHLEDQdITHVPAENRHVNTVFQSYALFPH-------MSVF 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKGS-VAYVPQQAWIQNDSLRENILFGKalnekyyQQVL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGLRMQKTPAAEITprvldalrmvqleEFAQrKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 181
Cdd:TIGR00957 735 EACALLPDLEILPSGDRT-------------EIGE-KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490998897 182 NELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:TIGR00957 801 EHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-231 |
5.32e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKT---VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVDSGRIHLEDQdITHVPaenrHVNTVFQSyalf 95
Cdd:PLN03232 623 SWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-VAYVP----QVSWIFNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 phmSVFENVAFGLRMQKT---PAAEITP--RVLDALRMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:PLN03232 694 ---TVRENILFGSDFESErywRAIDVTAlqHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 171 ALDYKLRKQ-----MQNELKalqrklGITFVFVThDQEEALTMSDRIVVMRDGKIEQDGTPREIYE 231
Cdd:PLN03232 770 ALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-232 |
7.58e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvpAENRHVNTVFQ- 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPH-MSVFENVAfglrmQKTPAAEITPRVLDAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:PRK15064 391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 169 LSALDYKLRKQMQNELKALQrklGiTFVFVTHDQEEALTMSDRIVVMRDGKIEQ-DGTpreiYEE 232
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGT----YEE 522
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-225 |
8.06e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.52 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--NVDSGRIHLEDQDITHVPAENRH-- 84
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 -VNTVFQSYALFPHMSV--FENVAFGLRMQKTPAAEITPR-----VLDALRMVQLEE-FAQRKPHQ-LSGGQQQRVAIAR 154
Cdd:CHL00131 85 gIFLAFQYPIEIPGVSNadFLRLAYNSKRKFQGLPELDPLefleiINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 155 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEealtMSDRIV-----VMRDGKIEQDGT 225
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR----LLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-232 |
9.73e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVDSGRIHLEDQdITHVPaenrHVNTVFQSyalfphmSVFE 102
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-VAYVP----QVSWIFNA-------TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 NVAFGL-----RMQKTPAAEITPRVLDALRMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 177
Cdd:PLN03130 698 NILFGSpfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 178 KQMQNelKALQRKL-GITFVFVThDQEEALTMSDRIVVMRDGKIEQDGTpreiYEE 232
Cdd:PLN03130 777 RQVFD--KCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----YEE 825
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-216 |
4.24e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAENRhVNTVFQSYAL---FPHM 98
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 sVFENVAFG----LRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 174
Cdd:PRK15056 97 -VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490998897 175 KLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMR 216
Cdd:PRK15056 176 KTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-225 |
5.01e-14 |
|
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: 70.90 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 33 TINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPaenRHVNTVFQsyalfphMSVFEnvafgLRMQK 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 113 TPAAEITPRV-LDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKL 191
Cdd:cd03237 86 TKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190
....*....|....*....|....*....|....
gi 490998897 192 GITFVFVTHDQEEALTMSDRIVVMrDGKIEQDGT 225
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-182 |
1.36e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 68.74 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEnrHVNTVFQSYALFPHMSVFEN 103
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 104 VAFGLRMQKTpaAEITPRvldALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 182
Cdd:PRK13541 91 LKFWSEIYNS--AETLYA---AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-228 |
1.78e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG--LENVD-SGRIHLEDQDIThvpAENRHVNTVF--QSYALFPHM 98
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrsPKGVKgSGSVLLNGMPID---AKEMRAISAYvqQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 99 SVFENVAFG--LRMQK-TPAAEITPRVLDALRMVQLEEFAQRK---PHQ---LSGGQQQRVAIARAVVNKPRLLLLDESL 169
Cdd:TIGR00955 115 TVREHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 170 SALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGKIEQDGTPRE 228
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-193 |
2.76e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKT---VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLED----QDItHVPAENRH 84
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 85 VNTVFQSYALFPHmSVFENVAFGLR----------------------------------------MQKTPAAEIT----- 119
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 120 ------PRVLDALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK---LRKQ 179
Cdd:PTZ00265 541 yqtikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQK 620
|
250
....*....|....
gi 490998897 180 MQNELKALQRKLGI 193
Cdd:PTZ00265 621 TINNLKGNENRITI 634
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
30-248 |
3.52e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN----VDSGRIHLEDQDITHVPAENRH------VNTVFQ--SYALFPH 97
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRklvghnVSMIFQepQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 98 MSVFENVA---------------FGLRmqKTPAAEITPRV-----LDALRMVqleefaqrkPHQLSGGQQQRVAIARAVV 157
Cdd:PRK15093 106 ERVGRQLMqnipgwtykgrwwqrFGWR--KRRAIELLHRVgikdhKDAMRSF---------PYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 158 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 237
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPY 254
|
250
....*....|.
gi 490998897 238 VASFIGEINLF 248
Cdd:PRK15093 255 TQALIRAIPDF 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-220 |
3.93e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 14 LAGIRKSFDGKTV--ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIA----GLENVDSGRIH---LEDQDIT-HVPAEnr 83
Cdd:TIGR00956 62 FRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITydgITPEEIKkHYRGD-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 84 hVNTVFQSYALFPHMSVFENVAFGLRMqKTPAAeitpRVLDALRmvqlEEFAQRKPH----------------------Q 141
Cdd:TIGR00956 140 -VVYNAETDVHFPHLTVGETLDFAARC-KTPQN----RPDGVSR----EEYAKHIADvymatyglshtrntkvgndfvrG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 142 LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTHDQ--EEALTMSDRIVVMRDGK 219
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAYELFDKVIVLYEGY 288
|
.
gi 490998897 220 I 220
Cdd:TIGR00956 289 Q 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-220 |
4.52e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 4 QPRSLSP-LVQLAGIrksfDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT-HVPAE 81
Cdd:PRK11288 249 RPRPLGEvRLRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 NRHVNTVF-----QSYALFPHMSVFENVAFGLRMQKTPA---------AEITPRVLDALRMvqleefAQRKPHQ----LS 143
Cdd:PRK11288 325 AIRAGIMLcpedrKAEGIIPVHSVADNINISARRHHLRAgclinnrweAENADRFIRSLNI------KTPSREQlimnLS 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 144 GGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-227 |
5.80e-13 |
|
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: 69.83 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 30 LNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIThvpAENR-----HVNTVFQSYALFPHMsvfenv 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNReayrqLFSAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 105 afgLRMQKTPAAEITPRVLDALRM---VQLE--EFAQRKphqLSGGQQQRVAIARAVV-NKPrLLLLDEslSALD----- 173
Cdd:COG4615 422 ---LGLDGEADPARARELLERLELdhkVSVEdgRFSTTD---LSQGQRKRLALLVALLeDRP-ILVFDE--WAADqdpef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 174 ----YklrKQMQNELKAlqrkLGITFVFVTHDqEEALTMSDRIVVMRDGKIEQDGTPR 227
Cdd:COG4615 493 rrvfY---TELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-219 |
8.22e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 14 LAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDI---THVPAENRHVNTVFQ 90
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 91 SYALFPHMSVFENVAFGLRMQKTPAAEI------TPRVLDALrmvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdTKAIFDEL---DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 165 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGK 219
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-224 |
2.32e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDQDITHVPAENRHVNTV 88
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYALFPHMSVFENVAFglrMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQL---------------SGGQQQRVAIA 153
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFF---LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 154 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQE-EALTMSDRIVVMRDGKIEQDG 224
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-234 |
5.21e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTViSDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDIT-HVP-----------AENRHVNT 87
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPldavkkgmayiTESRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 VFQSYALFPHMSVFENV-------AFGL---RMQKTPAAEitPRVLDALRMVQLEEfaqrKPHQLSGGQQQRVAIARAVV 157
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLkdggykgAMGLfheVDEQRTAEN--QRELLALKCHSVNQ----NITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 158 NKPRLLLLDESLSALD-------YKLRKQMQNElkalqrklGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIY 230
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDvgakaeiYKVMRQLADD--------GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
....
gi 490998897 231 EEPK 234
Cdd:PRK09700 498 SEEE 501
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-232 |
8.79e-12 |
|
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: 64.88 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVD-----SGRIHLEDQDITHVPAenrhvntvfqsyalfp 96
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEgkikhSGRISFSSQFSWIMPG---------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 97 hmSVFENVAFGLRMQKTpaaeitpRVLDALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:cd03291 113 --TIKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 166 DESLSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:cd03291 184 DSPFGYLDVFTEKEIFEScvCKLMANK---TRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-218 |
1.13e-11 |
|
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: 62.01 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvpaenrhVNtvfqsyalfphmsvfenvafglrmqktpaa 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------ID------------------------------ 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 117 eiTPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ-----NELKALQRKL 191
Cdd:smart00382 38 --GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|..
gi 490998897 192 GITFVFVTHDQEEALTM-----SDRIVVMRDG 218
Cdd:smart00382 116 NLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-223 |
1.34e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKT-TVLRLIAGLENVDSGRIHLE-------------DQDITHVPaENRhvntv 88
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDgkpvkirnpqqaiAQGIAMVP-EDR----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 fQSYALFPHMSVFENVAFGLRMQKTPAAeitpRVLDALRMVQLEEFAQR------KPHQ----LSGGQQQRVAIARAVVN 158
Cdd:PRK13549 348 -KRDGIVPVMGVGKNITLAALDRFTGGS----RIDDAAELKTILESIQRlkvktaSPELaiarLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 159 KPRLLLLDESLSALD----YKLRKQMqNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 223
Cdd:PRK13549 423 NPKILILDEPTRGIDvgakYEIYKLI-NQLV----QQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-220 |
1.66e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 11 LVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEdQDITHVPAEN---RHVNT 87
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 88 vfqsyalfphmSVFENVAFGLRMQktpaAEITPRVLDALRMV----------QLEEFAQRKPHQ---------------- 141
Cdd:PRK11147 82 -----------TVYDFVAEGIEEQ----AEYLKRYHDISHLVetdpseknlnELAKLQEQLDHHnlwqlenrinevlaql 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 142 ----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDR 211
Cdd:PRK11147 147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATR 222
|
....*....
gi 490998897 212 IVVMRDGKI 220
Cdd:PRK11147 223 IVDLDRGKL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-201 |
1.77e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFD-GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLenvdsgrihleDQDIT--HVPAENRHVNTVF 89
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNgeARPQPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQK--------------TPAAEitprvLDAL--RMVQLEEF------------------A 135
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKdaldrfneisakyaEPDAD-----FDKLaaEQAELQEIidaadawdldsqleiamdA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 136 QRKP------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHD 201
Cdd:TIGR03719 150 LRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPG-TVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-173 |
3.18e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDqdithvpaenrhvnTVFQSY--- 92
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------------TVKLAYvdq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ---ALFPHMSVFENVAFGLRMQKTPAAEITPRvldalrmvqleefA------------QRKPHQLSGGQQQRVAIARAVV 157
Cdd:PRK11819 395 srdALDPNKTVWEEISGGLDIIKVGNREIPSR-------------AyvgrfnfkggdqQKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 490998897 158 NKPRLLLLDESLSALD 173
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-223 |
4.49e-11 |
|
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: 64.08 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGL-ENVDSGRIHLE-------------DQDITHVPaENRhvntvfQSY 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINgkpvdirnpaqaiRAGIAMVP-EDR------KRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 ALFPHMSVFENV------AFGLRMQKTPAAEITPrVLDALRMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLL 165
Cdd:TIGR02633 349 GIVPILGVGKNItlsvlkSFCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 166 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQD 223
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-220 |
9.49e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 23 GKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGrihledqdithvpaenrhvnTVFQSYALfpHMSVF- 101
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--------------------TVFRSAKV--RMAVFs 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFGLRMQKTP---AAEITPRVLDALRMVQLEEF------AQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 172
Cdd:PLN03073 579 QHHVDGLDLSSNPllyMMRCFPGVPEQKLRAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 173 DYKLRKQMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PLN03073 659 DLDAVEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-267 |
2.10e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAG-LENVD-----SGRIHLEDQDITHVPAenrhvntvfqsya 93
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkikhSGRISFSPQTSWIMPG------------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 94 lfphmSVFENVAFGLRMQKTpaaeitpRVLDALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRL 162
Cdd:TIGR01271 502 -----TIKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 163 LLLDESLSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDGKIEQDGTPREIYEEPKNlFVAS 240
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESclCKLMSNK---TRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAKRPD-FSSL 644
|
250 260 270
....*....|....*....|....*....|.
gi 490998897 241 FIGEINlFNATVIER----LDEQRVRASVEG 267
Cdd:TIGR01271 645 LLGLEA-FDNFSAERrnsiLTETLRRVSIDG 674
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-205 |
2.42e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 10 PLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGlenvD------------------------- 64
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----Dhpqgysndltlfgrrrgsgetiwdi 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 65 -------SGRIHLEDQDITHVpaenrhVNTVFQSYalFPHMSVFENVAFGLRMqktpaaeITPRVLDALRMVqlEEFAQR 137
Cdd:PRK10938 335 kkhigyvSSSLHLDYRVSTSV------RNVILSGF--FDSIGIYQAVSDRQQK-------LAQQWLDILGID--KRTADA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 138 KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTHDQEEA 205
Cdd:PRK10938 398 PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD------------PLNRQLVRRFVdvlisegetqllFVSHHAEDA 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-173 |
2.87e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIH----LEdqdITHvpaenrhvntvFQSY--A 93
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtkLE---VAY-----------FDQHraE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 94 LFPHMSVFENVAFGLRmqktpaaEIT----PR-VLDALRMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:PRK11147 394 LDPEKTVMDNLAEGKQ-------EVMvngrPRhVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDE 466
|
....*.
gi 490998897 168 SLSALD 173
Cdd:PRK11147 467 PTNDLD 472
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-214 |
3.45e-10 |
|
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: 61.34 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 9 SPLVQLAGIRKSFDGKTVISDLNlTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHlEDQDITHVPAEnrhvntV 88
Cdd:COG1245 339 ETLVEYPDLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKPQY------I 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 89 FQSYalfpHMSVFENvafgLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:COG1245 411 SPDY----DGTVEEF----LRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490998897 169 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVV 214
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMV 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-232 |
3.53e-10 |
|
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: 61.89 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTV-LRLIAGLENVDsGRIHLEDQDITHVPAEN--RHVNTVFQSYALFphmsvfe 102
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 103 nvAFGLRMQKTPAAEITPR-VLDALRMVQLEEFAQRKP----HQ-------LSGGQQQRVAIARAVVNKPRLLLLDESLS 170
Cdd:TIGR00957 1373 --SGSLRMNLDPFSQYSDEeVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 171 ALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSdRIVVMRDGKIEQDGTPREIYEE 232
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-222 |
4.88e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVlRLIAGLENVDSGRihlEDQDITHVPAENRHVNTVFQS 91
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 92 Y-----ALFPHMSVFENVAFGLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:NF000106 90 Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 167 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEA------LTMSDRIVVMRDGKIEQ 222
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDE 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-237 |
5.13e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHMsvfen 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGT----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 vafgLRMQKTPAAEITPRVL-DALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:PLN03232 1326 ----VRFNIDPFSEHNDADLwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 172 LDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 237
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-214 |
7.90e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 5 PRSLS---PLVQLAGIRKSFDGKTVISDlNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLE---------- 71
Cdd:PRK13409 331 PRDESereTLVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 72 --DQDIThVPAENRHVNTVFQSyalfphmSVFENvafglrmqktpaaEItprvldaLRMVQLEEFAQRKPHQLSGGQQQR 149
Cdd:PRK13409 410 kpDYDGT-VEDLLRSITDDLGS-------SYYKS-------------EI-------IKPLQLERLLDKNVKDLSGGELQR 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVV 214
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMV 526
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-221 |
3.02e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 4 QPRSL-SPLVQLAGIRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLedqdithvpAEN 82
Cdd:PRK10636 304 APESLpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQsyalfpHMSVFenvafgLRMQKTP---AAEITPRVLDAlrmvQLEEF----------AQRKPHQLSGGQQQR 149
Cdd:PRK10636 375 IKLGYFAQ------HQLEF------LRADESPlqhLARLAPQELEQ----KLRDYlggfgfqgdkVTEETRRFSGGEKAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 150 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGKIE 221
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-201 |
2.58e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 13 QLAGIRKSFDG-KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLenvdsgrihleDQDIT--HVPAENRHVNTVF 89
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFEgeARPAPGIKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 90 QSYALFPHMSVFENVAFGLRMQK--------------TPAAEitprvLDAL--RMVQLEEF------------------A 135
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGVAEVKaaldrfneiyaayaEPDAD-----FDALaaEQGELQEIidaadawdldsqleiamdA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 136 QRKPH------QLSGGQQQRVAIARAVVNKPRLLLLDESlsaldyklrkqmQNELKA---------LQRKLGiTFVFVTH 200
Cdd:PRK11819 152 LRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEP------------TNHLDAesvawleqfLHDYPG-TVVAVTH 218
|
.
gi 490998897 201 D 201
Cdd:PRK11819 219 D 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-242 |
6.81e-08 |
|
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: 52.99 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 3 IQPRSLSPLVQLAG--------IRKSFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQD 74
Cdd:cd03288 5 ISGSSNSGLVGLGGeikihdlcVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 75 ITHVPAEN--RHVNTVFQSYALFphmsvfenvAFGLRMQKTPAAEIT-PRVLDALRMVQLEEFAQRKPHQL--------- 142
Cdd:cd03288 85 ISKLPLHTlrSRLSIILQDPILF---------SGSIRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvtegge 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 143 --SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN-ELKALQRKlgiTFVFVTHDQEEALTmSDRIVVMRDGK 219
Cdd:cd03288 156 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250 260
....*....|....*....|...
gi 490998897 220 IEQDGTPREIYEEPKNLFvASFI 242
Cdd:cd03288 232 LVECDTPENLLAQEDGVF-ASLV 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-220 |
8.03e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAeNRHVNTVF-------QSYALFPHMS 99
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA-NEAINHGFalvteerRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 100 V-FENVAFGLRMQKTPAAEI--------TPRVLDALRMvqleefaqRKP-HQ-----LSGGQQQRVAIARAVVNKPRLLL 164
Cdd:PRK10982 343 IgFNSLISNIRNYKNKVGLLdnsrmksdTQWVIDSMRV--------KTPgHRtqigsLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998897 165 LDESLSALD-------YKLRKQMQNELKalqrklGItfVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PRK10982 415 LDEPTRGIDvgakfeiYQLIAELAKKDK------GI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-232 |
1.18e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDlNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITH---------VPAENRHVNTVFqsy 92
Cdd:PRK10938 15 DTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeqlqklVSDEWQRNNTDM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 93 alfphMSVFENvAFGlrmqKTPAAEITPRVLDALRMVQLEEFAQ------RKPHQLSGGQQQRVAIARAVVNKPRLLLLD 166
Cdd:PRK10938 91 -----LSPGED-DTG----RTTAEIIQDEVKDPARCEQLAQQFGitalldRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998897 167 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEE 232
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-222 |
2.41e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDsGRIHledqdITHVPAENRHVNTVFQSYALFPHMSVF 101
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQ-----IDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 102 ENVAFglRMQKTPAAEITP----RVLD--ALRMVqLEEFAQRKPHQ-------LSGGQQQRVAIARAVVNKPRLLLLDES 168
Cdd:TIGR01271 1304 FSGTF--RKNLDPYEQWSDeeiwKVAEevGLKSV-IEQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 169 LSALDyklrkqmQNELKALQRKLGITF----VFVTHDQEEALTMSDRIVVMRDGKIEQ 222
Cdd:TIGR01271 1381 SAHLD-------PVTLQIIRKTLKQSFsnctVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-261 |
2.75e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIhledqDITHVPAenrhvnTVFQSYALFPHMSVFENVAF 106
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAA------LIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 -GLRM--QKTPAAEITPRVLDalrMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:PRK13545 109 kGLMMglTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 184 LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREIYEEpknlfVASFIGEINLFNATVIERLDEQRV 261
Cdd:PRK13545 186 MNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKYNQMSVEERKDFREEQI 257
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-173 |
5.38e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.55 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 24 KTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLEN--VDSGRIHLEDQDIThvPAENRHVNTVFQSYALFPHMSVF 101
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 102 ENVAFglrmqktpAAeitprvldALRMVQLEefaQRKphqlsggqqqRVAIARAVVNKPRLLLLDESLSALD 173
Cdd:cd03232 98 EALRF--------SA--------LLRGLSVE---QRK----------RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
16-216 |
1.56e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 16 GIRKSFDGKTVIsdlnlTINNGEFLTLLGPSGCGKTTVLRLIAglenvdsgrihledqdithvpaenrhvntvfqsYALF 95
Cdd:cd03227 5 GRFPSYFVPNDV-----TFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALG 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 96 PHMSVFENVAFGLRMQKTPAAEITPRVLDalrmvqleefaqrkpHQLSGGQQQRVAIARAVVN---KPR-LLLLDESLSA 171
Cdd:cd03227 47 GAQSATRRRSGVKAGCIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslKPRpLYILDEIDRG 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490998897 172 LDyklrkqMQNELKAL-----QRKLGITFVFVTHDQEEALtMSDRIVVMR 216
Cdd:cd03227 112 LD------PRDGQALAeaileHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-214 |
1.83e-06 |
|
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: 47.57 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 34 INNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPaenrhvntvfqsyalfphmsvfenvafglrmQKT 113
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------------------QYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 114 paaeitprvldalrmvqleefaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGI 193
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 490998897 194 TFVFVTHDQEEALTMSDRIVV 214
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-215 |
2.65e-06 |
|
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: 48.13 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAGLENVDSGRiHLEDQDITHVPAENRhvNTVFQSYalfphmsvFENVAFG-LRMQKTPA 115
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFR--GSELQNY--------FTKLLEGdVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 116 -AEITPRVLDA------------------LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 176
Cdd:cd03236 95 yVDLIPKAVKGkvgellkkkdergkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 490998897 177 RKQMQNELKALQRKLGITFVfVTHDQEEALTMSDRIVVM 215
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCL 212
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-260 |
4.12e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHledqdithvpaENRHVNTVFQSYALFPHMSVFENVAF 106
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 GLRMQKTPAAEITPRVLDALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 186
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998897 187 LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGKIEQDGTPREI---YEEPKNLFVASFIGEINLFNatviERLDEQR 260
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDFKKKSKAEQKEFR----NKLDESR 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-222 |
4.67e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 22 DGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDsGRIHLEDQDITHVPAENRHvntvfQSYALFPH-MSV 100
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQkVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 101 FENVafgLRMQKTP----AAEITPRVLD--ALRMVqLEEFAQRKPHQL-------SGGQQQRVAIARAVVNKPRLLLLDE 167
Cdd:cd03289 89 FSGT---FRKNLDPygkwSDEEIWKVAEevGLKSV-IEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490998897 168 SLSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGKIEQ 222
Cdd:cd03289 165 PSAHLDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-237 |
1.02e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVPAEN--RHVNTVFQSYALFPHmSVFEN 103
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VafglrmqkTPAAEITP-RVLDALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPR-LLLLDESLS 170
Cdd:PTZ00243 1404 V--------DPFLEASSaEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998897 171 ALDYKLRKQMQNE-LKALQRKLGITFVFVTHdqeeALTMSDRIVVMRDGKIEQDGTPREIYEEPKNLF 237
Cdd:PTZ00243 1476 NIDPALDRQIQATvMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-229 |
1.48e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 26 VISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAGLENVDSGRIHLEDQDITHVP-AENRHVNTVF-QSYALFPHmsvfeN 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIpQAPVLFSG-----T 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 104 VAFGLrmqkTPAAEITPRVL-DALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:PLN03130 1329 VRFNL----DPFNEHNDADLwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998897 172 LDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGKIEQDGTPREI 229
Cdd:PLN03130 1405 VDVRtdalIQKTIREEFKS------CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-215 |
2.72e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAG-----LENVDsgrihlEDQDITHVPaeNRHVNTVFQSYalfphmsvFENVAFG-LR- 109
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnLGDYE------EEPSWDEVL--KRFRGTELQNY--------FKKLYNGeIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 110 MQKTPAAEITPRVL-----DALRMV-------------QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:PRK13409 163 VHKPQYVDLIPKVFkgkvrELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 172 LDYKLRKQMQNELKALQRklGITFVFVTHDqeeaLT----MSDRIVVM 215
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
44-72 |
3.29e-05 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 43.24 E-value: 3.29e-05
10 20 30
....*....|....*....|....*....|..
gi 490998897 44 GPSGCGKTTVLRLIA---GLENVDSGRIHLED 72
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTEE 37
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-215 |
4.07e-05 |
|
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: 45.55 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAG-----LENVDSgrihledqdithvPAENRHVNTVFQSYALFPHmsvFENVAFG-LRM 110
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGelkpnLGDYDE-------------EPSWDEVLKRFRGTELQDY---FKKLANGeIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 111 -QKTPAAEITPRVLD--------------ALRMV----QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 171
Cdd:COG1245 163 aHKPQYVDLIPKVFKgtvrellekvdergKLDELaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490998897 172 LDYKLRKQMQNELKALQRKlGITFVFVTHDqeeaLT----MSDRIVVM 215
Cdd:COG1245 243 LDIYQRLNVARLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
82-236 |
4.73e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 82 NRHVNTVF---QSYALFPHMSVFENVAF----GLRMQKTPAA-----EITPRvLDALRMVQLEEFA-QRKPHQLSGGQQQ 148
Cdd:TIGR00630 417 KPEALAVTvggKSIADVSELSIREAHEFfnqlTLTPEEKKIAeevlkEIRER-LGFLIDVGLDYLSlSRAAGTLSGGEAQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 149 RVAIARAV------VnkprLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM------R 216
Cdd:TIGR00630 496 RIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIgpgageH 569
|
170 180
....*....|....*....|
gi 490998897 217 DGKIEQDGTPREIYEEPKNL 236
Cdd:TIGR00630 570 GGEVVASGTPEEILANPDSL 589
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-218 |
5.13e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 37 GEFLTLLGPSGCGKTTVLRLIAglENVDSGRIHLEDQDITHVPAEN---RHVNTVFQSYALFPHMSVFENVAFGLRM--- 110
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 111 QKTPAAEITPRVLDALRMVQLEEFAQR---KPHQ-LSGGQQQRVAIARAVVNKPRLLL-LDESLSALDyklrKQMQNELK 185
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 490998897 186 ALQRKL---GITFVFVTHdQEEALTMS--DRIVVMRDG 218
Cdd:TIGR00956 943 KLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-215 |
1.85e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 27 ISDLNLTINNGEFLTLLGPSGCGKTTVLrliaglenvdsgrihledQDITHVPAENRHVNTVfqsyALFPHmsvfenvaf 106
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV------------------NEGLYASGKARLISFL----PKFSR--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 107 glrmQKTPAAEITPRVLD-ALRMVQLEefaqRKPHQLSGGQQQRVAIAR--AVVNKPRLLLLDESLSALDYKLRKQMQNE 183
Cdd:cd03238 60 ----NKLIFIDQLQFLIDvGLGYLTLG----QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|..
gi 490998897 184 LKALqRKLGITFVFVTHDqEEALTMSDRIVVM 215
Cdd:cd03238 132 IKGL-IDLGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-220 |
3.22e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 142 LSGGQQQRVAIARAVVNKPRLLLLDESLSALD-------YKLRKQMQNELKALqrklgitfVFVTHDQEEALTMSDRIVV 214
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyeiYTIINELAAEGKGV--------IVISSELPELLGMCDRIYV 476
|
....*.
gi 490998897 215 MRDGKI 220
Cdd:NF040905 477 MNEGRI 482
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
286-366 |
4.46e-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: 38.37 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 286 VLLRPEDLRVDEvhdgsDADGLIGYIRERNYKGMTLESVVELENGKMVMVSEFFNEDDPdfdHPLDQKMAINWVESWEVV 365
Cdd:pfam08402 1 LAIRPEKIRLAA-----AANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHV 72
|
.
gi 490998897 366 L 366
Cdd:pfam08402 73 L 73
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-260 |
6.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 20 SFDGKTVISDLNLTINNGEFLTLLGPSGCGKTTVLRLIAgLENVDS-----GRIHLE---------------DQDITHVP 79
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDGipkncQILHVEqevvgddttalqcvlNTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 80 AENRHVNTVFQSYAL-FPHMSVFENVAFGLRMQKTPA----AEITPRvLDALRMVQLE--------------EFAQRKPH 140
Cdd:PLN03073 265 LLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVsqrlEEIYKR-LELIDAYTAEaraasilaglsftpEMQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 141 QLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGKI 220
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490998897 221 eqdgtpreiyeepknlfvASFIGEINLFNATVIERLDEQR 260
Cdd:PLN03073 420 ------------------VTYKGDYDTFERTREEQLKNQQ 441
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
12-218 |
4.09e-03 |
|
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: 37.97 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 12 VQLAGIRkSFDGKTVIsdlnltinngEF---LTLL-GPSGCGKTTVLR-----LIAGLENVDSGRIHleDQDITHVPAEN 82
Cdd:cd03240 4 LSIRNIR-SFHERSEI----------EFfspLTLIvGQNGAGKTTIIEalkyaLTGELPPNSKGGAH--DPKLIREGEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998897 83 RHVNTVFQS-----YALFPHMSVFENVAFglrmqktpaaeitprvldaLRMVQLEEFAQRKPHQLSGGQQQ------RVA 151
Cdd:cd03240 71 AQVKLAFENangkkYTITRSLAILENVIF-------------------CHQGESNWPLLDMRGRCSGGEKVlasliiRLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998897 152 IARAVVNKPRLLLLDESLSALD-YKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIV-VMRDG 218
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIYrVEKDG 199
|
|
| |
