|
Name |
Accession |
Description |
Interval |
E-value |
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-378 |
0e+00 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 784.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 4 SKKLNKQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH 83
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 VPAENRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVV 163
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 164 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 243
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 244 VAGFIGEINMFNATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDNHAEGLIGYVRERNYK 323
Cdd:PRK09452 241 VARFIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 324 GMTLESVVELENGKMVMVSEFFNEDDPDFDHSLDQKMAINWVESWEVVLADEEHK 378
Cdd:PRK09452 321 GMTLDSVVELENGKMVMVSEFFNEDDPDFDHSLGQKVAVTWVEGWEVVLADEEHK 375
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-372 |
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: 578.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 48 LLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR 127
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 128 VMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 207
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 208 QEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNATVIERLDEQRVRANVEGRECNIYVNFAVEPG 287
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 288 QKLHVLLRPEDLRVEEINDDNHAEGLIGYVRERNYKGMTLESVVELENGKMVMVSEFFNEDDPDFDHSLDQKMAINWVES 367
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPHMSPSIGDRVGLTWHPG 320
|
....*
gi 16129089 368 WEVVL 372
Cdd:TIGR01187 321 SEVVL 325
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
15-374 |
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: 530.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTV 94
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 175 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMF 254
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 255 NATVIERlDEQRVRanVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDNhaeGLIGYVRERNYKGMTLESVVELE 334
Cdd:COG3842 243 PGTVLGD-EGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPEN---GLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16129089 335 NGKMVMVSEFFNEDDPdfdHSLDQKMAINWVESWEVVLAD 374
Cdd:COG3842 317 DGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-307 |
3.26e-152 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 432.96 E-value: 3.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGE--INMFN 255
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 256 ATVIE---RLDEQRVRANVEGrecniyvnfAVEPGQKLHVLLRPEDLRVEEINDD 307
Cdd:COG3839 244 GTVEGggvRLGGVRLPLPAAL---------AAAAGGEVTLGIRPEHLRLADEGDG 289
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-249 |
1.44e-147 |
|
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: 416.64 E-value: 1.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIG 249
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-320 |
1.44e-133 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 385.65 E-value: 1.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENRYVNTVFQ 96
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 177 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNA 256
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 257 TVIErldeqrvrANVEGRECNIYVNFAVEPGQKlHVLLRPEDLRV-EEINDDNHAEGLIGYVRER 320
Cdd:COG1118 243 RVIG--------GQLEADGLTLPVAEPLPDGPA-VAGVRPHDIEVsREPEGENTFPATVARVSEL 298
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
14-335 |
1.18e-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: 355.50 E-value: 1.18e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 14 LSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNT 93
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINM 253
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 254 FNAtviERLDEQRVRANVEGRECNiyvNFAVEPGQKLHVLLRPEDLRVEEIndDNHAEGLIGYVRERNYKGMTLESVVEL 333
Cdd:TIGR03265 241 LPG---TRGGGSRARVGGLTLACA---PGLAQPGASVRLAVRPEDIRVSPA--GNAANLLLARVEDMEFLGAFYRLRLRL 312
|
..
gi 16129089 334 EN 335
Cdd:TIGR03265 313 EG 314
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-230 |
5.89e-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: 343.35 E-value: 5.89e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-315 |
1.08e-112 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 332.96 E-value: 1.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGK-EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHV-PAEnRYVNTVF 95
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 176 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGE--INM 253
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 254 FNATVierLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLR--------------VEEINDDNHAEGLIG 315
Cdd:PRK11650 243 LDGRV---SADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIAlssaeggvpltvdtVELLGADNLAHGRWG 315
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-250 |
6.81e-110 |
|
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: 321.21 E-value: 6.81e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQK----TPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGE 250
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-339 |
2.54e-109 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 324.87 E-value: 2.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 8 NKQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE 87
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 168 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGF 247
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 248 IGEINMFNATVIERLDEQRVrANVEGRECNIYVN--FAVEPGQKLHVLLRPEDLRV-EEINDD--NHAEGLIGYVRernY 322
Cdd:PRK11607 250 IGSVNVFEGVLKERQEDGLV-IDSPGLVHPLKVDadASVVDNVPVHVALRPEKIMLcEEPPADgcNFAVGEVIHIA---Y 325
|
330
....*....|....*..
gi 16129089 323 KGMTLESVVELENGKMV 339
Cdd:PRK11607 326 LGDLSIYHVRLKSGQMI 342
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-230 |
5.56e-107 |
|
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: 313.04 E-value: 5.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-257 |
1.30e-106 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 317.05 E-value: 1.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNAT 257
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-229 |
1.70e-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: 295.46 E-value: 1.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 12 SSLSPLVQLAGIRKCF----DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE 87
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVntvFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:COG1116 82 RGVV---FQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 168 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 229
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-258 |
2.05e-97 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 293.91 E-value: 2.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRM----QKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINM 253
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 16129089 254 FNATV 258
Cdd:PRK10851 243 LQGTI 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-306 |
5.91e-96 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 290.39 E-value: 5.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 178 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINM---- 253
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMnflp 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 254 --FNATVIERL-----DEQRVRANVEGRecniyvnfAVEPGQKLHVLLRPEDLRVEEIND 306
Cdd:PRK11000 244 vkVTATAIEQVqvelpNRQQVWLPVEGR--------GVQVGANMSLGIRPEHLLPSDIAD 295
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-226 |
1.05e-94 |
|
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: 282.05 E-value: 1.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGK----EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVnt 93
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 vFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03293 79 -FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 226
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
36-249 |
2.21e-89 |
|
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: 268.82 E-value: 2.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGLR 115
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 MQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQR 195
Cdd:cd03299 98 KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 196 KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIG 249
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
38-300 |
6.99e-87 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 268.12 E-value: 6.99e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE------NRYVNTVFQSYALFPHMTVFENVA 111
Cdd:COG4175 48 FDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALLPHRTVLENVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 191
Cdd:COG4175 128 FGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 192 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEIN----------MFNATVIER 261
Cdd:COG4175 208 ELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDrskvltagsvMRPPEAVVS 287
|
250 260 270
....*....|....*....|....*....|....*....
gi 16129089 262 LDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLR 300
Cdd:COG4175 288 EKDGPRVALRRMREEGISSLYVVDRDRRLLGVVTADDAL 326
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-229 |
1.09e-83 |
|
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: 1.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCF-DGKEVIPQL---DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE--- 87
Cdd:COG1136 2 SPLLELRNLTKSYgTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 ---NRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVN 164
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 165 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRIEQD 229
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-250 |
1.49e-82 |
|
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: 251.84 E-value: 1.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCF-DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTV 94
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE--TFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 172
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 173 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGE 250
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-248 |
5.69e-82 |
|
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: 251.41 E-value: 5.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN------RYVNTVFQSYALFPHMTVFENV 110
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 AFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 190
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 191 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFI 248
Cdd:cd03294 204 LRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-240 |
2.92e-80 |
|
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: 254.83 E-value: 2.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 9 KQPSSLSPLVQLAGIRKCFD--GKEVIPQLD---LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH 83
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYPvrGKGGVRAVDdvsLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 VPAEN-----RYVNTVFQ--SYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQ 154
Cdd:COG1123 332 LSRRSlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 155 RVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....*.
gi 16129089 235 IYEEPK 240
Cdd:COG1123 492 VFANPQ 497
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-235 |
5.17e-78 |
|
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: 239.88 E-value: 5.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY----- 90
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
17-241 |
1.71e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 236.04 E-value: 1.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNT--- 93
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 -VFQSYALFPHMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:COG1126 81 mVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 172 DESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:COG1126 161 DEPTSALD----PELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-226 |
6.97e-76 |
|
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: 233.92 E-value: 6.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFD-GKEVIPQL---DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE------ 87
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 168 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRI 226
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-264 |
1.15e-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: 238.21 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 25 KCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHV-PAENRYVN-----TVFQSY 98
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRrkkigMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 179 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNATV 258
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
....*.
gi 16129089 259 IERLDE 264
Cdd:TIGR01186 241 AERIAQ 246
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
37-250 |
2.76e-74 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 230.41 E-value: 2.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGLRm 116
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 117 qktPAAEITP----RVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVV-NKPrLLLLDESLSALDYKLRKQMQNELK 191
Cdd:COG3840 98 ---PGLKLTAeqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 192 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGE 250
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-230 |
5.31e-73 |
|
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: 226.41 E-value: 5.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINnGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIML------DNEDITHVPAENRYVNTVFQSYALFPHMTVFE 108
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRmqKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 188
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16129089 189 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-226 |
2.51e-72 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 226.28 E-value: 2.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHvPAENRYVntVFQSYALFPHMTVFEN 109
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:COG4525 97 VAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQEL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 16129089 190 LKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 226
Cdd:COG4525 177 LLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-242 |
7.71e-72 |
|
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: 223.75 E-value: 7.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQS--YALFpH 103
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 184 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-235 |
1.85e-71 |
|
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: 223.15 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY-----VN 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 172 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-225 |
5.76e-71 |
|
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: 219.75 E-value: 5.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT----HVPAENRYVNT 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 VFQSYALFPHMTVFENVAFGLrmqktpaaeitprvmealrmvqletfaqrkphqlSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-314 |
3.77e-70 |
|
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: 223.82 E-value: 3.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNED------ITHVPAENRYVNTVFQSYALFPHMTVFE 108
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRmqKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 188
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 189 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNATVIERLDEQR-V 267
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGlT 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 268 RANVEGREcnIYVNF-AVEPGQKL-------HVLL---RPEDL--------RVEEINDDNHAEGLI 314
Cdd:COG4148 255 RLALGGGR--LWVPRlDLPPGTRVrvrirarDVSLalePPEGSsilnilpgRVVEIEPADGGQVLV 318
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-241 |
4.98e-70 |
|
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: 220.06 E-value: 4.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 21 AGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP--AENRYVNTVFQSY 98
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 --ALFPHMTVFENVAFGLRMQKTPaaEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:COG1124 89 yaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 176 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:COG1124 167 SALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-230 |
6.23e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 213.76 E-value: 6.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQSYALFP 102
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:COG2884 93 DRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 183 RKQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:COG2884 173 SWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
36-230 |
3.78e-66 |
|
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: 209.28 E-value: 3.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR-----YVNTVFQSY--ALFPHMTVFE 108
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkEIQMVFQDPmsSLNPRMTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRMQK--TPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 185
Cdd:cd03257 104 QIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 186 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03257 184 ILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-226 |
8.31e-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: 205.07 E-value: 8.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH----VPAENRYVNT 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 VFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 172
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 173 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-238 |
5.06e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 204.14 E-value: 5.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYVNTVFQ 96
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 177 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-242 |
7.52e-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: 212.07 E-value: 7.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDG--KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGL---ETVDSGRIMLDNEDITHVPAENR 89
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 --YVNTVFQS--YALFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:COG1123 82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
30-225 |
2.52e-63 |
|
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: 201.54 E-value: 2.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY--VNTVFQsyalFP-HM-- 104
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQ----NPdDQff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 --TVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:cd03225 90 gpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129089 183 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:cd03225 170 RRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-238 |
4.13e-63 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 202.21 E-value: 4.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCF-DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----R 89
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYALFPHMTVFENVAFG-----------LRMQktPAAEItPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAI 158
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLF--PPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 159 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
27-235 |
1.86e-62 |
|
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: 200.66 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHM 104
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:COG1120 91 TVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-274 |
6.27e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.84 E-value: 6.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGK----EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP-----AEN 88
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 RYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 169 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeealtMS------DRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260 270
....*....|....*....|....*....|..
gi 16129089 243 FVAGFIGEInmFNATVIERLDEQRVRANVEGR 274
Cdd:COG1135 236 LTRRFLPTV--LNDELPEELLARLREAAGGGR 265
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
37-240 |
1.12e-60 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 198.42 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQ-SYA-LFPHMTVFEN 109
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGLRMQK-TPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 187
Cdd:COG4608 118 IAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 188 NELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:COG4608 198 NLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-240 |
1.21e-59 |
|
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: 192.80 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCF-DGKEVIPQLD---LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP-----AE 87
Cdd:cd03258 1 MIELKNVSKVFgDTGGKVTALKdvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 168 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-241 |
1.42e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 187.61 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYV----N 92
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 172 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-223 |
4.34e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 185.38 E-value: 4.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGleTVD-----SGRIMLDNEDITHVPAENRYVNTVFQSYALFP 102
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLSpafsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLRmQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:COG4136 90 HLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129089 183 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRD 223
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-233 |
1.32e-56 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 185.65 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 10 QPSSL---SPLVqLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA 86
Cdd:PRK11247 3 NTARLnqgTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 87 ENRYVntvFQSYALFPHMTVFENVAFGLRMQKTPAAEitprvmEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKP 166
Cdd:PRK11247 82 DTRLM---FQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 167 RLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT---PR 233
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTvdlPR 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-238 |
3.67e-56 |
|
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: 183.92 E-value: 3.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQSYALFP 102
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLRMQKT---------PAAEItPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03256 92 RLSVLENVLSGRLGRRStwrslfglfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-237 |
4.42e-56 |
|
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: 195.05 E-value: 4.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqktpAAEITP-RVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:COG2274 565 IRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 174 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPREIYE 237
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-239 |
7.24e-56 |
|
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: 186.86 E-value: 7.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI------THVPAENRYVNTVFQSYALFPHMTVFEN 109
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGlrMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:TIGR02142 96 LRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129089 190 LKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
36-230 |
1.79e-55 |
|
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: 181.15 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGLr 115
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 mqkTPAAEITP----RVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 191
Cdd:cd03298 96 ---SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 16129089 192 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-242 |
2.51e-55 |
|
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: 182.63 E-value: 2.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDneDITHVPAENRY-----VNTVFQSyalfPH-----MT 105
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLWeirkkVGMVFQN----PDnqfvgAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 185
Cdd:TIGR04520 95 VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 186 MQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:TIGR04520 175 VLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
15-235 |
7.03e-55 |
|
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: 181.00 E-value: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY---- 90
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTvFQSYALFPHMTVFENVA---------------FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQR 155
Cdd:COG0411 82 ART-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 156 VAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
36-240 |
7.23e-55 |
|
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: 182.95 E-value: 7.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE---TVDSGRIMLDNEDITHVPAEN------RYVNTVFQ-SY-ALFPHM 104
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElrkirgREIQMIFQdPMtSLNPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRM-QKTPAAEITPRVMEALRMVQL---ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:COG0444 104 TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQdGTPREIYEEPK 240
Cdd:COG0444 184 TIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEE-GPVEELFENPR 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-234 |
8.78e-55 |
|
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: 179.94 E-value: 8.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 11 PSSLSPLVQLAGIRKCFDGKE----VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA 86
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 87 E------NRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIAR 160
Cdd:COG4181 82 DararlrARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 161 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPRE 234
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-235 |
1.01e-54 |
|
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: 179.68 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETV-----DSGRIMLDNEDI----THVPAEN 88
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 RYVNTVFQSYALFPhMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL-ETFAQR-KPHQLSGGQQQRVAIARAVVNK 165
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-224 |
1.40e-54 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 180.28 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnRYVntVFQ 96
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-RGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 177 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 224
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-238 |
1.23e-53 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 177.36 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYVNTVF 95
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 176 SALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-251 |
2.12e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.00 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGK----EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP-----AEN 88
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 RYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 169 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFI 248
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
...
gi 16129089 249 GEI 251
Cdd:PRK11153 242 QST 244
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-226 |
1.06e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 19 QLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQ 96
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPhMTVFENVAFGLRMQKTPAAEitPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129089 176 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
28-238 |
1.64e-52 |
|
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: 174.79 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQSYALFP 102
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFG-LRMQKT--------PAAEITpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:TIGR02315 93 RLTVLENVLHGrLGYKPTwrsllgrfSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-235 |
1.65e-52 |
|
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: 174.16 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY---VNTVFQSY 98
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ALFPHMTVFENVAFGLRMQKTPA----------AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 169 LLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-239 |
2.41e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.12 E-value: 2.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTV 94
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPhMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:COG1121 84 AEVDWDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 171 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEqDGTPREIYEEP 239
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-224 |
4.53e-52 |
|
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: 173.04 E-value: 4.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHvPAENRYVntVFQSYALFPHMTVFENVAFGLR 115
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 --MQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKAL 193
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 16129089 194 QRKLGITFVFVTHDQEEALTMSDRIVVMRDG 224
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-235 |
1.88e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 171.30 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGL 114
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 RmqktPAAEITP----RVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 190
Cdd:PRK10771 97 N----PGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 191 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-261 |
1.94e-51 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 176.76 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP-AENRYVN-----TVFQSYALFPHMTVFENVA 111
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 191
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 192 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINM---FNATVIER 261
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIsqvFSAKDIAR 281
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
36-240 |
6.58e-51 |
|
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: 177.95 E-value: 6.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTT----VLRLIAGletvdSGRIMLDNEDITHVPAEN-----RYVNTVFQS-YA-LFPHM 104
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRMQKTP--AAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:COG4172 380 TVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 182 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQdGTPREIYEEPK 240
Cdd:COG4172 460 VQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ-GPTEQVFDAPQ 518
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-226 |
1.04e-50 |
|
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: 167.57 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR-YVNTVFQ 96
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVafglrmqktpaaeitprvmealrmvqletfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129089 177 ALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-240 |
1.08e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 167.11 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE--DITHVPAEN------R 89
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYALFPHMTVFEN-VAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 169 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTpREIYEEPK 240
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-234 |
2.85e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 174.58 E-value: 2.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqktpAAEITP-RVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:COG1132 430 IRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 174 SLSALDYKLRKQMQNELKALQRklGITFVFVTHDqeeaLT---MSDRIVVMRDGRIEQDGTPRE 234
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTHEE 560
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
16-240 |
4.47e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 166.13 E-value: 4.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--------HVPAE 87
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgeLVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNT-------VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIA 159
Cdd:COG4598 87 RRQLQRirtrlgmVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 160 RAVVNKPRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 236
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALD----PELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
....
gi 16129089 237 EEPK 240
Cdd:COG4598 243 GNPK 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-240 |
7.11e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.19 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE--DITHVPAEN------R 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALA---RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTpREIYEEPK 240
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
36-226 |
1.02e-48 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 163.73 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH-----VPAENRYVNTVFQSYALFPHMTVFENV 110
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQDFRLLPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 AFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 190
Cdd:cd03292 100 AFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 16129089 191 KALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03292 180 KKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
27-230 |
4.79e-48 |
|
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: 160.68 E-value: 4.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQsyalfphm 104
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 tvfenvafglrmqktpaaeitprvmeALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 184
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16129089 185 QMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-239 |
2.24e-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: 169.18 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 10 QPSSLSPLVQLAGIRKCFDG--KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE 87
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 N--RYVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAeitprVMEALRMVQLETFAQRKPH-----------QLSGGQQQ 154
Cdd:COG4987 406 DlrRRIAVVPQRPHLF-DTTLRENLRLA-RPDATDEE-----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 155 RVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPR 233
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHE 554
|
....*.
gi 16129089 234 EIYEEP 239
Cdd:COG4987 555 ELLAQN 560
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-238 |
6.73e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 161.37 E-value: 6.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE----NRYVNTVFQ--SYALFPH 103
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 mTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL--ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 182 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-225 |
1.03e-46 |
|
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: 158.41 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYVNTV 94
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPHMTVFENVAFGLRMQKTPAAEItpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 175 LSALDyklrKQMQNELKAL---QRKLGITFVFVTHDQEEALtmSDRIVVMRDGR 225
Cdd:COG4133 159 FTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-221 |
4.93e-46 |
|
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: 156.92 E-value: 4.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPhMTV 106
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FENVAFGL----RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:cd03235 88 RDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 16129089 183 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVM 221
Cdd:cd03235 168 QEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-237 |
1.23e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 157.87 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRI-----MLDNEDITHVpaeNRYVNTVFQSY-ALFPHMTVFENVA 111
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmVLSEETVWDV---RRQVGMVFQNPdNQFVGATVQDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 191
Cdd:PRK13635 105 FGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16129089 192 ALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYE 237
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
28-238 |
1.39e-45 |
|
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: 164.16 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlRMQKTPAAeitprVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:COG4988 427 IRENLRLG-RPDASDEE-----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-236 |
2.11e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 157.20 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--HVPAENRYVNTVFQSY-ALFPHMTVFENVAFGLRM 116
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDDVAFGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 117 QKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRK 196
Cdd:PRK13650 110 KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129089 197 LGITFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIY 236
Cdd:PRK13650 190 YQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-225 |
2.62e-45 |
|
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: 153.31 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVafglrmqktpaaeitprvmealrmvqletfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 185
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129089 186 MQNELKALQRklGITFVFVTHDqEEALTMSDRIVVMRDGR 225
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-249 |
2.76e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.06 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI----------THVPAE 87
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKP 166
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 167 RLLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN---- 241
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQprtr 241
|
....*...
gi 16129089 242 LFVAGFIG 249
Cdd:PRK11264 242 QFLEKFLL 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-173 |
2.77e-45 |
|
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: 152.80 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH--VPAENRYVNTVFQSYALFPHMTVFENVAFG 113
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 114 LRMQKTPAAEITPRVMEALRMVQLETFAQRK----PHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-225 |
6.81e-45 |
|
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: 152.01 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 19 QLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnryvntvfqsy 98
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 alfphmtvfenvafglrmqktpaaeitprvmEALRMVQLEtfaqrkpHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:cd00267 70 -------------------------------ELRRRIGYV-------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16129089 179 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-235 |
1.00e-44 |
|
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: 153.74 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 19 QLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------Yvn 92
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 tVFQSYALFPHMTVFENVAFGLRMQKtpAAEITPRVMEALRMV-QLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:cd03224 80 -VPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 172 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
30-231 |
1.47e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.84 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQSY--ALFP 102
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK10419 105 RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 231
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-234 |
1.97e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 154.12 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP----AENRYVntVFQSYAL-FPh 103
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelARRRAV--LPQHSSLaFP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARA-------VVNKPRLLLLDESLS 176
Cdd:COG4559 90 FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 177 ALDykLRKQmQNELKALqRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:COG4559 170 ALD--LAHQ-HAVLRLA-RQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-240 |
6.32e-44 |
|
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: 151.93 E-value: 6.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------YVNtvf 95
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgigYLP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 176 SALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-235 |
2.05e-43 |
|
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: 150.21 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYVNTVFQ 96
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 177 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
30-226 |
5.26e-43 |
|
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: 150.73 E-value: 5.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQ-SYALF-P 102
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPSAVnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLET-FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-235 |
1.15e-42 |
|
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: 148.04 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKE--VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENRYVNTV 94
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 175 LSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-241 |
7.74e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.11 E-value: 7.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLETvdSGRIMLDNEDI----THVPAENRYVNTVF 95
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIydpdVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPhMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMV--------QLETFAQRkphqLSGGQQQRVAIARAVVNKP 166
Cdd:COG1117 99 QKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAalwdevkdRLKKSALG----LSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 167 RLLLLDESLSALD-----------YKLRKQMqnelkalqrklgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG1117 174 EVLLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
....*.
gi 16129089 236 YEEPKN 241
Cdd:COG1117 241 FTNPKD 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-237 |
2.91e-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: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRmqktpaaEITP-RVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03251 92 VAENIAYGRP-------GATReEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 174 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 237
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-230 |
4.08e-41 |
|
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: 144.27 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEvIPQLD---LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHV-PAE-NRYVN 92
Cdd:cd03245 3 IEFRNVSFSYPNQE-IPALDnvsLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFpHMTVFENVAFGLrmqktPAAEiTPRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARA 161
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 162 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-240 |
9.45e-41 |
|
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: 150.61 E-value: 9.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDG----KEVIPQLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGLETVDSGRIMLDNEDITHVPA 86
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 87 E-------NRyVNTVFQ--SYALFPHMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQL---ETFAQRKPHQLSGGQQ 153
Cdd:COG4172 84 RelrrirgNR-IAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 154 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLT----MSDRIVVMRDGRIEQD 229
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQ 238
|
250
....*....|.
gi 16129089 230 GTPREIYEEPK 240
Cdd:COG4172 239 GPTAELFAAPQ 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
22-240 |
1.58e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 143.25 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------YVNtvf 95
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigYLP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:COG1137 85 QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 176 SALDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:COG1137 165 AGVDPIAVADIQKIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-230 |
3.63e-40 |
|
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: 141.18 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGeFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY-VNTVFQ 96
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 177 ALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-226 |
3.84e-40 |
|
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: 141.20 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQS 97
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPHMTVFENVAFGLRMQKTPAAeitpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16129089 178 LDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-240 |
3.89e-40 |
|
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: 142.04 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR----- 89
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 -YVNtvfQSYALFPHMTVFEN--VAFGLRMQKTPAAEITPRVMEalRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKP 166
Cdd:COG0410 81 gYVP---EGRRIFPSLTVEENllLGAYARRDRAEVRADLERVYE--LFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 167 RLLLLDE-SLsALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:COG0410 156 KLLLLDEpSL-GLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-267 |
4.05e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.92 E-value: 4.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCF-----DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR--Y 90
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSYAL--FPHMTVFENVA--------FGLRMQKTPA--AEITPRVmEALRMvQLETFAQRKPHQLSGGQQQRVAI 158
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKrrELFRELL-ATLGL-GLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 159 ARAVVNKPRLLLLDESLSALDYKlRKQMQNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD--Gtprei 235
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDvsG----- 233
|
250 260 270
....*....|....*....|....*....|..
gi 16129089 236 yEEPKNLFVAGFigeINMFNATVIERLDEQRV 267
Cdd:COG1101 234 -EEKKKLTVEDL---LELFEEIRGEELADDRL 261
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-235 |
7.17e-40 |
|
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: 141.76 E-value: 7.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSG---RIM---LDNEDIthvpAEN 88
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDV----WEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 R----YVNTVFQSYaLFPHMTVFENVAFGL-----RMQKTPAAEITpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIA 159
Cdd:COG1119 77 RkrigLVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 160 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
1.05e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.14 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH----VPAENRYVNTVFQSY--ALF 101
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkksLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 102 PHmTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 182 LRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-240 |
1.39e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 143.31 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY-----VNTVFQS--YALFPHMTVFEN 109
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGLRM--QKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 186
Cdd:PRK15079 121 IAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 187 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK15079 201 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
29-234 |
1.47e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 141.06 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP----AENRYVntVFQSYAL-FPh 103
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelARRRAV--LPQHSSLsFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVV------NKPRLLLLDESLSA 177
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 178 LDykLRKQMQ--NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:PRK13548 171 LD--LAHQHHvlRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-230 |
1.58e-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: 139.81 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQ----LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYV 91
Cdd:cd03266 1 MITADALTKRFRDVKKTVQavdgVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 172 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-231 |
2.93e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 139.57 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCF-DGK---EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA---- 86
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 87 --ENRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVN 164
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 165 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGT 231
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-238 |
6.54e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 140.22 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIM---LDNEDITHVPAENRYVNTVFQSyalfPH--- 103
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgLDTSDEENLWDIRNKAGMVFQN----PDnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 --MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK13633 99 vaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 182 LRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-239 |
1.76e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 138.74 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-----THVPAENRYV 91
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 171 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-238 |
1.97e-38 |
|
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: 137.67 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--HVPAENRYVNTVFQSYALFPhMTVFE 108
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGlrmqKTPAAEITprVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03249 96 NIRYG----KPDATDEE--VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 178 LDYKLRKQMQnelKALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:cd03249 170 LDAESEKLVQ---EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-226 |
1.27e-37 |
|
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: 132.94 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDithvpaenryvntvfqs 97
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 yalfphmtvfenVAFGlrmqktpaaeiTPRVMEAL--RMVqletfaqrkpHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:cd03216 64 ------------VSFA-----------SPRDARRAgiAMV----------YQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129089 176 SALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-241 |
1.64e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.12 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGK---------EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP 85
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 86 AENR--YVNTVFQ--SYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIA 159
Cdd:COG4167 82 YKYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 160 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
..
gi 16129089 240 KN 241
Cdd:COG4167 242 QH 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-237 |
9.63e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 135.32 E-value: 9.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 11 PSSLSPLvQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENR 89
Cdd:PRK13537 2 PMSVAPI-DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 237
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-238 |
1.12e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 135.73 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 2 GQSKKLNKQPSSLSPL-VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNED 80
Cdd:PRK13536 25 GISEAKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 81 ithVPAENRY----VNTVFQSYALFPHMTVFEN-VAFG--LRMQKTPAAEITPRVMEALRmvqLETFAQRKPHQLSGGQQ 153
Cdd:PRK13536 105 ---VPARARLararIGVVPQFDNLDLEFTVRENlLVFGryFGMSTREIEAVIPSLLEFAR---LESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 154 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 233
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
....*
gi 16129089 234 EIYEE 238
Cdd:PRK13536 258 ALIDE 262
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-226 |
1.34e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 138.61 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH---VPAENRYVN 92
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrspRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFPHMTVFENVAFGlRMQKTPA----AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLG-REPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 169 LLLDESLSALDYK----LRKQMqNELKALqrklGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:COG1129 162 LILDEPTASLTEReverLFRII-RRLKAQ----GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-239 |
1.36e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.77 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINngefLTL--------LGPSGCGKTTVLRLIAGLETVDSGRIML------DNEDITHVPAENRYVNTVFQSYAL 100
Cdd:PRK11144 12 DLCLTVN----LTLpaqgitaiFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 101 FPHMTVFENVAFGLRmqktpaaeitpRVMEAL--RMVQL---ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:PRK11144 88 FPHYKVRGNLRYGMA-----------KSMVAQfdKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 176 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-231 |
1.85e-36 |
|
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: 132.26 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 19 QLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------YVN 92
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaragiaYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 tvfQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEaLRMVqLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 172
Cdd:TIGR03410 82 ---QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 173 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 231
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
30-267 |
3.21e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 133.00 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY-----VNTVFQSY-ALFPH 103
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWdirekVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 184 KQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFigEINMFNaTVIERLD 263
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGL--DIPFVY-KLKNKLK 255
|
....
gi 16129089 264 EQRV 267
Cdd:PRK13640 256 EKGI 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-239 |
4.29e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 132.04 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP----AENRYV 91
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTvFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA-----AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRV 156
Cdd:PRK11300 84 RT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 157 AIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 236
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 16129089 237 EEP 239
Cdd:PRK11300 243 NNP 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-239 |
6.47e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.03 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCF-DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIM---LDNEDITHVPAENRYVN 92
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQS-YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 172 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
39-240 |
1.43e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.40 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-----NRYVNTVFQS-YA-LFPHMTVFENVA 111
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNPRKKVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGLRMQKT-PAAEITPRVMEALRMVQLET-FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:PRK11308 117 EPLLINTSlSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129089 190 LKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-226 |
1.96e-35 |
|
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: 128.91 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIthvPAENRY--VNTVFQS--YALFPH 103
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRksIGYVMQDvdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 mTVFENVAFGLRmqktPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:cd03226 88 -SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129089 184 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-245 |
3.74e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.11 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIThvpAEN-----RYVNTVFQSY-ALFPH 103
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENlkeirKKIGIIFQNPdNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:PRK13632 99 ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 184 KQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVA 245
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
22-240 |
6.88e-35 |
|
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: 128.16 E-value: 6.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY---VNTVFQSY 98
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:TIGR04406 86 SIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 178 LDYKLRKQMQNELKAL-QRKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLkERGIG---VLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-242 |
7.56e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.10 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQS-YALFPHMTVFENVAFGLRM 116
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGSIVKYDVAFGLEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 117 QKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRK 196
Cdd:PRK13648 112 HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16129089 197 LGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13648 192 HNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
36-247 |
8.35e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 129.44 E-value: 8.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIThvpAEN-----RYVNTVFQSY-ALFPHMTVFEN 109
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENvwnlrRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 190 LKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGF 247
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-226 |
1.24e-34 |
|
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: 125.41 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVpAENRY---VNTVFQSYALFPHmTVFE 108
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELgdhVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVafglrmqktpaaeitprvmealrmvqletfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 188
Cdd:cd03246 95 NI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 16129089 189 ELKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGRI 226
Cdd:cd03246 138 AIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-234 |
1.26e-34 |
|
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: 127.35 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqKTPAAEItpRVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:cd03253 91 IGYNIRYG----RPDATDE--EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPRE 234
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-241 |
1.50e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.16 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 23 IRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----------RYV 91
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NT----VFQSYALFPHMTVFENVAFG----LRMQKTPAAEitpRVMEALRMVQLETFAQRK-PHQLSGGQQQRVAIARAV 162
Cdd:PRK10619 91 RTrltmVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 163 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-235 |
5.66e-34 |
|
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: 126.06 E-value: 5.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE--NRYVNTVFQSYALFpHMT 105
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqkTPAAEITpRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:cd03252 92 IRDNIALA-----DPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-235 |
6.33e-34 |
|
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: 132.18 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmTVFEN 109
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAfglRMqktpaAEITP-RVMEALRMVQLETFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:COG4618 426 IA---RF-----GDADPeKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 178 LDYKLRKQMQNELKALqRKLGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:COG4618 498 LDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-238 |
8.29e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 126.28 E-value: 8.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 14 LSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDS----------------GRIMld 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqreGRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 78 nEDITHVPAENRYVntvFQSYALFPHMTVFENVAFGlRMQKTP---------AAEITPRVMEALRMVQLETFAQRKPHQL 148
Cdd:PRK09984 79 -RDIRKSRANTGYI---FQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 149 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 228
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|
gi 16129089 229 DGTPREIYEE 238
Cdd:PRK09984 234 DGSSQQFDNE 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-226 |
9.30e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.99 E-value: 9.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-----HVPAENRYVNTVFQSYALFPH 103
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129089 184 KQMQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK10908 174 EGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-226 |
1.81e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 123.54 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE--------DITHVPAENr 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 yvntvfqsyALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:cd03269 80 ---------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-235 |
1.96e-33 |
|
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: 130.61 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmT 105
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlRMQKTPAAEItprvMEALRMVQLETFAQRKP---HQ--------LSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR02203 422 IANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-267 |
2.67e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA-------ENRy 90
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 vntvfqsyALFPHMTVFENVAF-----GLrmqktPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:COG4152 81 --------GLYPKMKVGEQLVYlarlkGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE-PKNLFV 244
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLR 226
|
250 260
....*....|....*....|....*..
gi 16129089 245 AGFIGEI----NMFNATVIERLDEQRV 267
Cdd:COG4152 227 LEADGDAgwlrALPGVTVVEEDGDGAE 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
29-234 |
2.72e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 123.87 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmTV 106
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FENVAFGlrmqkTPAAEITpRVMEALRMVQLETFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:cd03254 94 MENIRLG-----RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 176 SALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-242 |
2.96e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.52 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT------HVPAENRYVNTVFQsyalFPHMTVFE-- 108
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQLFEet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 ---NVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 184
Cdd:PRK13634 103 vekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 185 QMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
28-235 |
5.26e-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: 5.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHV-PAE-NRYVNTVFQSYALFPHmT 105
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqkTPAAEITpRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR01846 547 IRDNIALC-----NPGAPFE-HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-233 |
5.29e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIThvpAENRY-----VNTVFQSY--AL 100
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKwvrskVGLVFQDPddQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 101 FPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK13647 93 FS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129089 181 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 233
Cdd:PRK13647 172 RGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-241 |
5.59e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.48 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGL-----ETVDSGRIMLDNEDITHVPAE--NRY 90
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSYALFPHMTVFENVAFGLRMQK--TPAAEITPRVMEALRMVQL-ETFAQR---KPHQLSGGQQQRVAIARAVVN 164
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 165 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-243 |
2.87e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.13 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 11 PSSLSPLVQLAGIRKCF-----------DGKEVIPQLDLTINNGEFLTLLGPSGCGKTT----VLRLIAGletvdSGRIM 75
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 76 LDNEDITH------VPAENRyVNTVFQ--SYALFPHMTVFENVAFGLRM-QKT-PAAEITPRVMEALRMVQLE-TFAQRK 144
Cdd:PRK15134 344 FDGQPLHNlnrrqlLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 145 PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 224
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250
....*....|....*....
gi 16129089 225 RIEQDGTPREIYEEPKNLF 243
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEY 521
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-238 |
1.61e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAenryvNTVFQSYALFP--HMT-- 105
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARRLALLPqhHLTpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 ---VFENVAFGlrmqKTP--------AAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:PRK11231 90 gitVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 175 LSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK11231 166 TTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-238 |
2.04e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 120.34 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH----VPAENRYVNTVFQS--YALF 101
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 102 PhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK13636 97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 182 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
28-221 |
2.25e-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: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY--VNTVFQSYALFPHmT 105
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRdqIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRMQktPAAEITprvmEALRMVQLETFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR02857 412 IAENIRLARPDA--SDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16129089 175 LSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTMsDRIVVM 221
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-238 |
3.87e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.60 E-value: 3.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDG----KEVipqlDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-HVPAE--N 88
Cdd:COG3845 4 PALELRGITKRFGGvvanDDV----SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 RYVNTVFQSYALFPHMTVFENVAFGL---RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 166 PRLLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG3845 160 ARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
36-234 |
4.84e-31 |
|
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: 124.16 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMTVFENVAFG 113
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 114 lRMQKTPAAeitprVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:COG5265 456 -RPDASEEE-----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 183 RKQMQNELKALQRklGITFVFVTH------DqeealtmSDRIVVMRDGRIEQDGTPRE 234
Cdd:COG5265 530 ERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-206 |
5.79e-31 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 123.76 E-value: 5.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldneditHVPAENRyvnTVF---QSYalFPHM 104
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPY--LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRMQKTPAAEITprvmEALRMVQLETFAQR------KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:COG4178 441 TLREALLYPATAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*....
gi 16129089 179 DYKLRKQMqneLKALQRKL-GITFVFVTH 206
Cdd:COG4178 517 DEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
43-241 |
6.46e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 123.81 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN-----RYVNTVFQS-YA-LFPHMTVFENVAFGLR 115
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 MQKT-PAAEITPRVMEALRMVQLE-TFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKAL 193
Cdd:PRK10261 430 VHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 194 QRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-241 |
8.01e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 118.02 E-value: 8.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVD-----SGRIMLDNEDITHV---PAE-NRYVNTVFQSYALF 101
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvdPIEvRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 102 PHMTVFENVAFGLRMQK--TPAAEITPRVMEALRMVQL-ETFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 176 SALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-238 |
1.49e-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: 122.22 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGkevipqLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSG----RIMLDNEDITHVPAENR-----YVN 92
Cdd:TIGR03269 295 GVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGRgrakrYIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFPHMTVFENV--AFGLRMQKTPAaeitprVMEALRMVQLETFAQRK--------PHQLSGGQQQRVAIARAV 162
Cdd:TIGR03269 369 ILHQEYDLYPHRTVLDNLteAIGLELPDELA------RMKAVITLKMVGFDEEKaeeildkyPDELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 163 VNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
46-242 |
1.87e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.60 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 46 LTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--HVPAENRYVNTVFQSY--ALFPhMTVFENVAFGLRMQKTPA 121
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNPddQIFS-PTVEQDIAFGPINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 122 AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITF 201
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTV 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129089 202 VFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13652 192 IFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-242 |
5.71e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 23 IRKCFDGK-----EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRI--MLDNEDITHVPAEN------- 88
Cdd:PRK13651 8 IVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 -----------------RYVNTVFQ--SYALFpHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQL 148
Cdd:PRK13651 88 viqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 149 SGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 228
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
250
....*....|....
gi 16129089 229 DGTPREIYEEPKNL 242
Cdd:PRK13651 246 DGDTYDILSDNKFL 259
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
36-238 |
8.04e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 116.00 E-value: 8.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH------VPAENRYVNTVFQsyalFPHMTVFE- 108
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESQLFEe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 ----NVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:PRK13649 102 tvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 184 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK13649 182 KELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-210 |
9.11e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.43 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnRY---V 91
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYrqqV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHmTVFENVAFGLRM-QKTPAAEitpRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIrNQQPDPA---IFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 210
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-235 |
1.09e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.02 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE--NRYVNT 93
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 VFQSYALFPHMTVFENVafglRMQKTP-------AAEITPRVME-ALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVV----EMGRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 166 PRLLLLDESLSALDykLRKQMQNelKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-234 |
1.26e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 14 LSPLVQLAGIRKCFDGKE----VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSG--RIM------LDNEDI 81
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAgqdvatLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 82 THVPAEnrYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARA 161
Cdd:PRK10535 81 AQLRRE--HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 162 VVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
30-235 |
1.53e-29 |
|
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: 119.37 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmTVF 107
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAfglRMQKTPAAEitpRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:TIGR01842 410 ENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 177 ALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-241 |
1.68e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGL-----ETVDSGRIMLDNEDI----THVP 85
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 86 AENRYVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEITPRVME-ALRMVQLETFAQRKPHQ----LSGGQQQRVAIAR 160
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 161 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 16129089 241 N 241
Cdd:PRK14239 240 H 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-239 |
3.93e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.59 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 12 SSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDS-----GRIMLDNEDI----T 82
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 83 HVPAENRYVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLETFAQRKPHQ----LSGGQQQRVA 157
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 158 IARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-----RDGRIEQDGTP 232
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLT 240
|
....*..
gi 16129089 233 REIYEEP 239
Cdd:PRK14258 241 KKIFNSP 247
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-226 |
4.04e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.84 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 7 LNKQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH--- 83
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 VPAENRYVNTVFQSYALFPHMTVFENVAFGLrmqktPAAEITPRVMEALrMVQLEtfAQRKPHQLSG----GQQQRVAIA 159
Cdd:PRK15439 81 AKAHQLGIYLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL-LAALG--CQLDLDSSAGslevADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 160 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-239 |
4.73e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.67 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVpaENRYVNT----VFQSYALFPHmT 105
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY--DHHYLHRqvalVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRmqKTPAAEItprvMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR00958 571 VRENIAYGLT--DTPDEEI----MAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 175 LSALDyklrKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:TIGR00958 645 TSALD----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-226 |
7.40e-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: 110.60 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-------------HVPaENRyvntvfQSYALFP 102
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdairagiaYVP-EDR------KREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFglrmqktpaaeitprvmealrmvqletfaqrkPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129089 183 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-229 |
1.35e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.41 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------YVNTVFQSYALFPHMTVFEN 109
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129089 190 LKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQD 229
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-252 |
1.63e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.68 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGL-ETVDS-----GRIMLDNEDITHVPA--ENRYVNTVFQSYA 99
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAikLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 100 LFPHMTVFENVAFGLRMQKTPAA-EITPRVMEALRMVQL--ETFAQ--RKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkEVYDRlnSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 175 LSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGF-IGEIN 252
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRIS 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-236 |
2.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDN-------EDITHVPAENRYVNTVFQ--SYALFPHmTVF 107
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 186
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129089 187 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 236
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-173 |
6.98e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 109.82 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 9 KQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPaEN 88
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLD-EH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 RYVNT----VFQSYALFPHMTVFENVAFGLRMQKTP--------AAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRV 156
Cdd:COG4674 81 EIARLgigrKFQKPTVFEELTVFENLELALKGDRGVfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWL 160
|
170
....*....|....*..
gi 16129089 157 AIARAVVNKPRLLLLDE 173
Cdd:COG4674 161 EIGMLLAQDPKLLLLDE 177
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-206 |
1.07e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 107.97 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRkcfDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnryvntvFQS 97
Cdd:PRK13538 5 RNLACER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALF--------PHMTVFENVAFGLRMQKTPAAEitpRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:PRK13538 75 DLLYlghqpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTH 206
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-235 |
1.64e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 109.31 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQ-LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHMT 105
Cdd:PRK10253 18 GKYTVAEnLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlRMQKTPA-----AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK10253 98 VQELVARG-RYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-235 |
2.59e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.06 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 25 KCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRY---VNTVFQSYALF 101
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 102 PHMTVFENVAFGLRMQKTPAAEI-TPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 181 KLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK10895 171 ISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-207 |
2.70e-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: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA-ENRYVNTVF-QSYALFpHMT 105
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCaQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlRMQKTPAAeitprVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR02868 425 VRENLRLA-RPDATDEE-----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 16129089 175 LSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHD 207
Cdd:TIGR02868 499 TEHLDAETADELLEDLlAALSGR---TVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
16-236 |
6.53e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.32 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP------AENR 89
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 yvnTVFQSYALFPHmtvfENVAFGLRMQKTPAAEITPRVM------------EALR-MVQLETFAQR---KPHQLSGGQQ 153
Cdd:PRK11701 85 ---RLLRTEWGFVH----QHPRDGLRMQVSAGGNIGERLMavgarhygdiraTAGDwLERVEIDAARiddLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 154 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDGT- 231
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRvVESGLTd 237
|
250
....*....|
gi 16129089 232 -----PREIY 236
Cdd:PRK11701 238 qvlddPQHPY 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-230 |
8.01e-27 |
|
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: 106.08 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 6 KLNKQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNeDITHVP 85
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 86 AenryVNTVFQsyalfPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:cd03220 90 G----LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-250 |
9.02e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 107.18 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHvpAENRY----VNTVFQ--SYALFPHM 104
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--GDYSYrsqrIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLET-FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:PRK15112 105 RISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 183 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP-----KNLfVAGFIGE 250
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlheltKRL-IAGHFGE 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-251 |
1.41e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 107.10 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGL-----------ETVDSGRIMLDNEDITH 83
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrysgDVLLGGRSIFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 VpaeNRYVNTVFQSYALFPhMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLETFAQRK----PHQLSGGQQQRVAI 158
Cdd:PRK14271 99 F---RRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 159 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
250
....*....|....*..
gi 16129089 239 PKNL----FVAGFIGEI 251
Cdd:PRK14271 253 PKHAetarYVAGLSGDV 269
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-221 |
2.96e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldnediTHVPAenRYVNTVFQSYAL---FPh 103
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGG--ARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 179
Cdd:NF040873 72 LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16129089 180 YKLRKQMQNELKALQRKlGITFVFVTHDQEEALTmSDRIVVM 221
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-247 |
3.08e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.86 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH----VPAENRYVNTVFQSyalfP 102
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVF-----ENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PRK13638 87 EQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 178 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGF 247
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-242 |
3.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT------HVPAENRYVNTVFQsyalFPHMTVFE 108
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 N-----VAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:PRK13641 101 NtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 183 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-225 |
3.82e-26 |
|
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: 109.14 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDS--GRIMLDNEDI--THV-PAENRYV 91
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIrDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHMTVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLETFAQRKP-HQLSGGQQQRVAIARAVVNKP 166
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 167 RLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-225 |
6.71e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 104.05 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCF-----DGKE--VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE----DITH 83
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 vpAENRYV-----NT---VFQsyalF----PHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSG 150
Cdd:COG4778 82 --ASPREIlalrrRTigyVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 151 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLR---KQMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-179 |
1.09e-25 |
|
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: 102.44 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE-NRYVNTVFQSYALFPHMTV 106
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 107 FENVAFGLRMQKTPAAEItprvMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 179
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-237 |
1.54e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.58 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETV--DSGRIM-------------------- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 76 --------LDNEDI-------THVPAENRYVNTVFQ-SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLET 139
Cdd:TIGR03269 81 pcpvcggtLEPEEVdfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 140 FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 219
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 16129089 220 VMRDGRIEQDGTPREIYE 237
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-226 |
1.67e-25 |
|
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: 102.93 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVpaENRY----VNTVFQSYALFPHmTVF 107
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKYlhskVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGLrmQKTPaaeiTPRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:cd03248 106 DNIAYGL--QSCS----FECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129089 177 ALDYKLRKQMQnelKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03248 180 ALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
36-238 |
2.32e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.85 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRI--------MLDnedithvpaenryVNTVFQsyalfPHMTVF 107
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsaLLE-------------LGAGFH-----PELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 187
Cdd:COG1134 107 ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16129089 188 NELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:COG1134 187 ARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-235 |
6.76e-25 |
|
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: 106.36 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVP--AENRYVNTVFQSYALFPHmTV 106
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FENvafgLRMQKTPAAEITpRVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:TIGR01193 565 LEN----LLLGAKENVSQD-EIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 176 SALDYKLRKQMQNELKALQRKlgiTFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-179 |
9.35e-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: 100.26 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRkcfDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEdithvpAENRYVNTVFQS 97
Cdd:cd03231 4 DELTCER---DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG------PLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YALFPH-------MTVFENVAFGLRMQKTPAaeitprVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:cd03231 75 LLYLGHapgikttLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
....*....
gi 16129089 171 LDESLSALD 179
Cdd:cd03231 149 LDEPTTALD 157
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-206 |
1.08e-24 |
|
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: 98.77 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRI-MLDNEDITHVPAEnryvntvfqsyalfPHMTV 106
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLPQR--------------PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 fenvafG-LRmqktpaaeitprvmEALRmvqletfaqrKP--HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDyklr 183
Cdd:cd03223 78 ------GtLR--------------EQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD---- 123
|
170 180
....*....|....*....|...
gi 16129089 184 KQMQNELKALQRKLGITFVFVTH 206
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-179 |
1.08e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.95 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 20 LAGIRKcfdGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--HVPAENRYV---Ntv 94
Cdd:PRK13539 8 LACVRG---GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpDVAEACHYLghrN-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 fqsyALFPHMTVFENVAFGLRMQKTPAAEItprvMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:PRK13539 83 ----AMKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
....*
gi 16129089 175 LSALD 179
Cdd:PRK13539 155 TAALD 159
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-242 |
1.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHvPAENRYVNTVFQSYAL---FPHMTV 106
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYIRPVRKRIGMvfqFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FEN-----VAFGLRMQKTPAAEITPRVMEALRMVQLE-TFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK13646 99 FEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 242
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-235 |
1.64e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.02 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT--HVPAENRYVNTVFQSYALFPHMTV 106
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FENVAFGlrmqKTP--------AAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PRK10575 103 RELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 179 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-246 |
1.77e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.34 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN---RYVNTVFQSYALFPHMTVF 107
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAF-GLRMQKTPAAEITPRVMEALRMVQlETFAQRKpHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 186
Cdd:PRK11614 99 ENLAMgGFFAERDQFQERIKWVYELFPRLH-ERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 187 QNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI--EQDGTPREIYEEPKNLFVAG 246
Cdd:PRK11614 177 FDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDALLANEAVRSAYLGG 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-231 |
1.81e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGLETV-DSGRIMLDNEDITHVPAE-------NRyVNTVFQS 97
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQtlrgvrgNK-IAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 --YALFPHMTV----FENVAFGLRMQKTPA-AEItprvMEALRMVQLETFAQR---KPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:PRK15134 101 pmVSLNPLHTLekqlYEVLSLHRGMRREAArGEI----LNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 168 LLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDGT 231
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQNRA 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
36-265 |
2.47e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.11 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLeTVDSGRI----MLDNEDITHVPAE--NRY----VNTVFQS--YALFPH 103
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLPEKelNKLraeqISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD 179
Cdd:PRK09473 114 MRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 180 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFvagfigEINMFNAtvI 259
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY------SIGLLNA--V 265
|
....*.
gi 16129089 260 ERLDEQ 265
Cdd:PRK09473 266 PRLDAE 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-225 |
2.80e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDS--GRIMLDNEDIT--HV-PAENR 89
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQasNIrDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYALFPHMTVFENVAFGlrmqktpaAEITP-----------RVMEALRMVQLETFAQRKPHQLSGGQQQRVAI 158
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLG--------NEITPggimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 159 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-238 |
4.76e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN------RYVNTVFQsyalFPHMTVFE- 108
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQ----FPESQLFEe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 ----NVAFGLRMQKTPAAEITPRVMEALRMVQL-ETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:PRK13643 101 tvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 184 KQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-231 |
4.82e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.50 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 8 NKQPSSLSPLVQLAGIRKCFDGK-EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPA 86
Cdd:PRK13657 325 AIDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 87 EN--RYVNTVFQSYALFpHMTVFENvafgLRMQKTPAAEitPRVMEALRMVQLETFAQRKPH-----------QLSGGQQ 153
Cdd:PRK13657 405 ASlrRNIAVVFQDAGLF-NRSIEDN----IRVGRPDATD--EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 154 QRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVfVTHdQEEALTMSDRIVVMRDGRIEQDGT 231
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-231 |
4.82e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 103.37 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 8 NKQPSSLSPLVQLAGIrkCF----DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH 83
Cdd:PRK11160 329 TSTAAADQVSLTLNNV--SFtypdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 84 VPAEN--RYVNTVFQSYALFPHmTVFENvafgLRMQKTPAAEitPRVMEALRMVQLETFAQRKP----------HQLSGG 151
Cdd:PRK11160 407 YSEAAlrQAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 152 QQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ-MQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQiLELLAEHAQNK---TVLMITH-RLTGLEQFDRICVMDNGQIIEQG 555
|
.
gi 16129089 231 T 231
Cdd:PRK11160 556 T 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-226 |
6.07e-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: 97.62 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETV--DSGRIMLDNEDItHVPAENRYVNTVFQSYALFPHMTV 106
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 107 FENVAFglrmqktpAAEitprvmeaLRmvqletfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 186
Cdd:cd03213 100 RETLMF--------AAK--------LR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129089 187 QNELKALqRKLGITFVFVTHD-QEEALTMSDRIVVMRDGRI 226
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-241 |
1.40e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGLE----TVDSGRIMLD--NEDI----THVPAENRYVN-----TVFQS- 97
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEqaggLVQCDKMLLRrrSRQVielsEQSAAQMRHVRgadmaMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 -YALFPHMTVFENVAFGLRMQ----KTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLD 172
Cdd:PRK10261 114 mTSLNPVFTVGEQIAESIRLHqgasREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 173 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 241
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-242 |
1.73e-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: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETvDSGRIMLDNEDITHVP----AENR-YVNTvfQSYALFPhMTVFENV 110
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSaaelARHRaYLSQ--QQSPPFA-MPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 AFGLRmQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAV------VN-KPRLLLLDESLSALDYklr 183
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDV--- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 184 kQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYeEPKNL 242
Cdd:COG4138 167 -AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-230 |
1.88e-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: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEdithVPAENR-----YVNTVF-QSYALFPH 103
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRkkflrRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLR 183
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16129089 184 KQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-225 |
2.44e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 96.38 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLdNEDITHVPAENRYVNTvfqsyalfphmTVFENVAFGLR 115
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PGSIAYVSQEPWIQNG-----------TIRENILFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 MQKtpaaeitPRVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 184
Cdd:cd03250 92 FDE-------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16129089 185 Q-MQNELKALqRKLGITFVFVTHdQEEALTMSDRIVVMRDGR 225
Cdd:cd03250 165 HiFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
39-240 |
4.26e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 98.28 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLetVD-SGRIM-----LDNEDITHVPAENRY------VNTVFQS--YALFPHM 104
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMaekleFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLETFAQR---KPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:PRK11022 107 TVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 181 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-226 |
6.68e-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: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH-------------VPaENRyvntvf 95
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVP-EDR------ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAF--------GLRMQKTPAAEITPRVMEAL--RMVQLETFAQrkphQLSGGQQQRVAIARAVVNK 165
Cdd:COG1129 337 KGEGLVLDLSIRENITLasldrlsrGGLLDRRRERALAEEYIKRLriKTPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 166 PRLLLLDESLSALD-------YKLrkqMqNELKAlqRKLGItfVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:COG1129 413 PKVLILDEPTRGIDvgakaeiYRL---I-RELAA--EGKAV--IVISSELPELLGLSDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-227 |
7.66e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIML-DNEDITHVPAENRYVNtv 94
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQEELD-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 fqsyalfPHMTVFENVAFGLRMQKtpaaEITPRVMealrmvqLETF-----AQRKP-HQLSGGQQQRVAIARAVVNKPRL 168
Cdd:COG0488 392 -------PDKTVLDELRDGAPGGT----EQEVRGY-------LGRFlfsgdDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 169 LLLDE--------SLSALdyklrkqmqneLKALQRKLGiTFVFVTHDQE--EALTmsDRIVVMRDGRIE 227
Cdd:COG0488 454 LLLDEptnhldieTLEAL-----------EEALDDFPG-TVLLVSHDRYflDRVA--TRILEFEDGGVR 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-238 |
8.64e-23 |
|
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: 94.52 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--TVDSGRIMLDNEDITHVPAENRYVNTVFqsyalfphmt 105
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIF---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 vfenvafgLRMQKTPaaEITP-RVMEALRMVQlETFaqrkphqlSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 184
Cdd:cd03217 81 --------LAFQYPP--EIPGvKNADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 185 QMQNELKALqRKLGITFVFVTHDQEEALTM-SDRIVVMRDGRIEQDGtPREIYEE 238
Cdd:cd03217 142 LVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-226 |
1.40e-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: 94.65 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVD---SGRIMLDNEDIThvPAENRY-VNTVFQSYALFPHMT 105
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK--PDQFQKcVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFG--LRMQ-KTPAAEITPRV-MEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:cd03234 98 VRETLTYTaiLRLPrKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 182 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-247 |
1.72e-22 |
|
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: 99.70 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 14 LSPLVQLAGIRKCFD--GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENRY 90
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 171 LDESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLFVAGF 247
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-243 |
4.60e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVdSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMT 105
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGlrmqktpAAEITP-RVMEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:PRK11174 439 LRDNVLLG-------NPDASDeQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 174 SLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPkNLF 243
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-225 |
1.79e-21 |
|
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: 89.43 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGrimldnedithvpaenryvntvfqs 97
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 yalfphmtvfenvafglrmqktpaaeiTPRVMEALRMVQLEtfaqrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:cd03221 56 ---------------------------IVTWGSTVKIGYFE--------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 178 LDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-226 |
3.32e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-------------HVPaENRyvntv 94
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglsprerrrlgvaYIP-EDR----- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 fQSYALFPHMTVFENVAFGLRMQKtpaaEITPRVMeaLRMVQLETFAQRK----------PHQ----LSGGQQQRVAIAR 160
Cdd:COG3845 343 -LGRGLVPDMSVAENLILGRYRRP----PFSRGGF--LDRKAIRAFAEELieefdvrtpgPDTparsLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 161 AVVNKPRLLL-------LDESLSAldyklrkQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:COG3845 416 ELSRDPKLLIaaqptrgLDVGAIE-------FIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
30-230 |
3.34e-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: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR-YVNTVFQSYALFpHMTVFE 108
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSsLISVLNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVafGLRmqktpaaeitprvmealrmvqletfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 188
Cdd:cd03247 94 NL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16129089 189 EL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:cd03247 140 LIfEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-232 |
4.62e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.90 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--TVDSGRIMLDNEDITHVPAENR------YVntvFQSYA 99
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaragifLA---FQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 100 LFPHMTV--FENVAFGLRMQKT-PAAEITPRVMEALRMVQL-ETFAQRKPHQ-LSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:COG0396 88 EIPGVSVsnFLRTALNARRGEElSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 175 LSALDYKLRKQMQNELKALQRKlGITFVFVTHdQEEALTM--SDRIVVMRDGRIEQDGTP 232
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-216 |
6.38e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 33 IPQLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGLETvdSGRIMLDNEDI--THV-PAE-NRYVNTVFQSYALF 101
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyaPDVdPVEvRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 102 PHmTVFENVAFGLRMQ--KTPAAEITPRvmeALRMVQLETFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:PRK14243 104 PK-SIYDNIAYGARINgyKGDMDELVER---SLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129089 176 SALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSD 216
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-247 |
7.04e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.56 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 14 LSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE-DITHVPaenryvn 92
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 tvfQSYALFPHMTVfeNVAFGLRMQK-TPAAEITPrvmeALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:PRK09544 74 ---QKLYLDTTLPL--TVNRFLRLRPgTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 172 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMrDGRIEQDGTPREIYEEPKnlFVAGF 247
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-179 |
8.05e-21 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 89.52 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 11 PSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVpAENRY 90
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSYALFPHMTVFENVAF-----GLRMQKTPAAeitprvmeALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....
gi 16129089 166 PRLLLLDESLSALD 179
Cdd:PRK13543 156 APLWLLDEPYANLD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
8.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 4 SKKLNKQPSSLSP--LVQLAGIRKCFDGKE-----VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSG---- 72
Cdd:PRK13631 6 MKKKLKVPNPLSDdiILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 73 -------RIMLDNEDITHVPAE-------NRYVNTVFQ--SYALFPHmTVFENVAFG---LRMQKTPAAEITPRVMEalR 133
Cdd:PRK13631 86 gdiyigdKKNNHELITNPYSKKiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--K 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 134 MVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQnELKALQRKLGITFVFVTHDQEEALT 213
Cdd:PRK13631 163 MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLE 241
|
250 260
....*....|....*....|....*.
gi 16129089 214 MSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
36-234 |
1.39e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 93.11 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIThvpAENRY-----VNTVFQSYALFPHMTVFENv 110
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEdyrklFSAVFTDFHLFDQLLGPEG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 afglrmqKTPAAEITPRVMEALRM---VQLETFAQRKPhQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 187
Cdd:PRK10522 418 -------KPANPALVEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 188 NELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRI-EQDGTPRE 234
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERD 536
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-238 |
1.53e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 26 CFDGKEViPQLD---LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYAL 100
Cdd:PRK11176 350 TYPGKEV-PALRninFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 101 FpHMTVFENVAFGlRMQKTPAAEITprvmEALRMVQLETFAQRKPH-----------QLSGGQQQRVAIARAVVNKPRLL 169
Cdd:PRK11176 429 F-NDTIANNIAYA-RTEQYSREQIE----EAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 170 LLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-235 |
2.35e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 89.50 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVD--------SGRIMLDNEDITHVPAEN----RYVnTVF 95
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRlarlRAV-LPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPhMTVFENVAFGLRMQKTPAAEITPRVME----ALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVN------- 164
Cdd:PRK13547 91 AAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 165 --KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-232 |
2.91e-20 |
|
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: 88.32 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTV----LRLIagleTVDSGRIMLDNEDITHVPaenryVNTVFQSYALFPH 103
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIG-----LHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 104 mtvfENVAFG--LRMQKTPAAEITP-RVMEALRMVQLETFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLL 169
Cdd:cd03244 86 ----DPVLFSgtIRSNLDPFGEYSDeELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 170 LLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 232
Cdd:cd03244 162 VLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-207 |
2.46e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 20 LAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLD-NEDITHVPaenryvntvfQSY 98
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ALFPHMTVFENVAFGLR------------MQKTPAAEITPRVMEAL--RMVQLETFA-------------------QRKP 145
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELqeEFEALGGWEaearaeeilsglgfpeedlDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 146 HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklgITFVFVTHD 207
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-290 |
2.86e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNED---ITHVPAENRYVN 92
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 93 TVFQSYALFPHMTVFENVAFGLRMQK-------TPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNK 165
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 166 PRLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG-----RIEQDGTPREIY---- 236
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVrlmv 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 237 -EEPKNLFVAGFIGEINMFNATVIE-----RLDEQRVRAnvegrecniyVNFAVEPGQKL 290
Cdd:PRK09700 243 gRELQNRFNAMKENVSNLAHETVFEvrnvtSRDRKKVRD----------ISFSVCRGEIL 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-226 |
5.70e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENRYVNTVFQSY-----ALFPHMTVFENVA- 111
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrkrdGLVLGMSVKENMSl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 -----FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK- 184
Cdd:PRK10762 354 talryFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKe 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129089 185 --QMQNELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK10762 434 iyQLINQFKA----EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
30-209 |
1.16e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--TVDSGRIMLDNEDIThvpaenryvntvfqsyalfPHMTVF 107
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-------------------REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAfglRMQKTPAAeitprvMEALRMVQLET--FAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 185
Cdd:COG2401 104 DAIG---RKGDFKDA------VELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|....
gi 16129089 186 MQNELKALQRKLGITFVFVTHDQE 209
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHYD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-238 |
1.25e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIML-----DNEDIthvpAENRYVNTVFQSYALFPHMTVFENVA 111
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI----ATRRRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELK 191
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 192 ALQRKLGITfVFV-THDQEEALTmSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:NF033858 442 ELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
36-240 |
1.93e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKT-TVLRLI----AGLETVdSGRIMLDNEDITHVPAENRYVNTVFQS--YALFPHMTVFE 108
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQT-AGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRMQKTPAAEitPRVMEALRMVQLE---TFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQ 185
Cdd:PRK10418 101 HARETCLALGKPADD--ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 186 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-225 |
2.25e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEdithvpaENRYVNT- 93
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-------EMRFASTt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 ---------VFQSYALFPHMTVFENV-------AFGLRMQKTPAAeitpRVMEALRMVQLETFAQRKPHQLSGGQQQRVA 157
Cdd:PRK11288 75 aalaagvaiIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNY----EAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 158 IARAVVNKPRLLLLDE---SLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:PRK11288 151 IAKALARNARVIAFDEptsSLSAREIEQLFRVIRELRAEGRVI----LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-226 |
5.55e-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: 81.54 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 23 IRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-LETVDS--GRIMLDNEDI----THVPAENRYVNtvf 95
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVSveGDIHYNGIPYkefaEKYPGEIIYVS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 96 QSYALFPHMTVFENVAFGLRMQktpaaeitprvmeALRMVqletfaqRKphqLSGGQQQRVAIARAVVNKPRLLLLDESL 175
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK-------------GNEFV-------RG---ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 176 SALDYKLRKQMQNELKALQRKLGIT-FVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-239 |
6.16e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.15 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmTVF 107
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGlRMQKTP-----AAEITPRVMEALRMVQ-LETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK10789 407 NNIALG-RPDATQqeiehVARLASVHDDILRLPQgYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 182 LRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK10789 486 TEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-239 |
1.13e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLeTVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHMTVFENVAFG 113
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 114 LRmQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIArAVV------NKP--RLLLLDESLSALDYKLRKQ 185
Cdd:PRK03695 94 QP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 186 MQNELKALQRkLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:PRK03695 172 LDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-275 |
1.34e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNeditHVPAENRYVN-----TVF-QSYALFPHMTVFEN 109
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKEFarrigVVFgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 vaFGL--RMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 187
Cdd:COG4586 117 --FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 188 NELKALQRKLGITFVFVTHDQE--EALtmSDRIVVMRDGRIEQDGTP---REIYEEPKNLFV--AGFIGEINMFNATVIE 260
Cdd:COG4586 195 EFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLeelKERFGPYKTIVLelAEPVPPLELPRGGEVI 272
|
250
....*....|....*
gi 16129089 261 RLDEQRVRANVEGRE 275
Cdd:COG4586 273 EREGNRVRLEVDPRE 287
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
38-239 |
7.36e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.72 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLE----TVDSGRIMLDNEDITHVPAENRY------VNTVFQ--SYALFPHMT 105
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERRkiigreIAMIFQepSSCLDPSAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVafglrMQKTPAAEITPRVMEalrmvqleTFAQRK----------------------PHQLSGGQQQRVAIARAVV 163
Cdd:COG4170 108 IGDQL-----IEAIPSWTFKGKWWQ--------RFKWRKkraiellhrvgikdhkdimnsyPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 164 NKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 239
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
40-234 |
1.14e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVD---SGRIMLDNEDIThVPAENRYVNTVFQSYALFPHMTVFENVAFG--L 114
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREHLMFQahL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 RMQK-TPAAEITPRVMEALRMVQLETFAQRK---PHQ---LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ 187
Cdd:TIGR00955 127 RMPRrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 188 NELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGRIEQDGTPRE 234
Cdd:TIGR00955 207 QVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-273 |
1.36e-16 |
|
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: 78.60 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPaenRYVNTVFQsyalfphMTVFEnvafgLRMQK 118
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 TPAAEITPRV-MEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKL 197
Cdd:cd03237 86 TKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 198 GITFVFVTHDQEEALTMSDRIVVMrDGRIEQDGT--PREIYEEPKNLFVAgfigeinmfNATVIERLDEQ--RVRANVEG 273
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVanPPQSLRSGMNRFLK---------NLDITFRRDPEtgRPRINKLG 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-238 |
1.63e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDN---EDITHvPAENRYVNTVFQSYALFPHm 104
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSH-SVLRQGVAMVQQDPVVLAD- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENVAFGLRMQKTpaaeitpRVMEALRMVQLETFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:PRK10790 430 TFLANVTLGRDISEE-------QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-248 |
2.13e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 17 LVQLAGIRKCFDGKE--VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI-THVPAENRYVNT 93
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 94 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 174 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLFVAGFI 248
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYI 2166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
36-226 |
2.47e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENR------YVNTVFQSYALFPHMTVFEN 109
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvYLPEDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VA------FGLRMQKTPAAEITPRVMEAL--RMVQLETFAQRkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:PRK15439 362 VCalthnrRGFWIKPARENAVLERYRRALniKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 182 LRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK15439 438 ARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
31-232 |
2.80e-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: 76.68 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnryvnTVFQSYALFPH-MTVFEN 109
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-----DLRSSLTIIPQdPTLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VafgLRMQKTPAAEITPR-VMEALRMVQletfaqrKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY----KLRK 184
Cdd:cd03369 97 T---IRSNLDPFDEYSDEeIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYatdaLIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 185 QMQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 232
Cdd:cd03369 167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
33-224 |
3.16e-16 |
|
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: 76.99 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 33 IPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDN-----EDITHVPAENRYVNTVFQSYALFPHMTVF 107
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknesePSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGLRMQK------TPAAEITPRVmEALRMVQLETFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK 181
Cdd:cd03290 97 ENITFGSPFNKqrykavTDACSLQPDI-DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 182 LRKQMQNE--LKALQRKlGITFVFVTHdQEEALTMSDRIVVMRDG 224
Cdd:cd03290 175 LSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-281 |
6.00e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-HVPAENRY--V 91
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHMTVFENVAFGlRMQKTPAAEITPRVM--EA---LRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKP 166
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLG-REFVNRFGRIDWKKMyaEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 167 RLLLLDESLSAL-DYKLRK--QMQNELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGrieqdgtpreiyeepknlf 243
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESlfRVIRELKSQGR--GI--VYISHRLKEIFEICDDVTVFRDG------------------- 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16129089 244 vaGFIGE-----------INMFnatVIERLDEQRVRANVEGRECNIYVN 281
Cdd:PRK10762 218 --QFIAErevadltedslIEMM---VGRKLEDQYPRLDKAPGEVRLKVD 261
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-231 |
1.07e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.83 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 15 SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--TVDSGRIMLDNEDITHVPAENRY-- 90
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 -VNTVFQSYALFPHMTV--FENVAFGLRMQKTPAAEITPR-----VMEALRMVQL-ETFAQRKPHQ-LSGGQQQRVAIAR 160
Cdd:CHL00131 85 gIFLAFQYPIEIPGVSNadFLRLAYNSKRKFQGLPELDPLefleiINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 161 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEealtMSDRIV-----VMRDGRIEQDGT 231
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR----LLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
32-216 |
1.37e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.60 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITH-VPAENRYVNTVFQSYALFPHMTVFENV 110
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 AFGLRMQKTpAAEITprvmEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNEL 190
Cdd:PRK13540 96 LYDIHFSPG-AVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170 180
....*....|....*....|....*.
gi 16129089 191 KALQRKLGItfVFVTHDQEEALTMSD 216
Cdd:PRK13540 171 QEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-225 |
1.54e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDS--GRIMLDNEDITHvPAENRyVNTVFQSYALFPHMTVFENVAFG--LRMQK 118
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-QILKR-TGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 TPAAEITPRVMEA----LRMVQLE------TFAQrkphQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQN 188
Cdd:PLN03211 172 SLTKQEKILVAESviseLGLTKCEntiignSFIR----GISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*...
gi 16129089 189 ELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGR 225
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-235 |
1.76e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 70 DSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFpHMTVFENVAFGlrmQKTPAAEITPRvmeALRMVQLETFAQRKPHQ 147
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlrNLFSIVSQEPMLF-NMSIYENIKFG---KEDATREDVKR---ACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 148 -----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSD 216
Cdd:PTZ00265 1348 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426
|
170 180
....*....|....*....|....
gi 16129089 217 RIVVM----RDGR-IEQDGTPREI 235
Cdd:PTZ00265 1427 KIVVFnnpdRTGSfVQAHGTHEEL 1450
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
36-233 |
2.41e-15 |
|
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: 77.15 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIThvpAENR--YVN---TVFQSYALFPHMtvfenv 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNReaYRQlfsAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 111 aFGLRMQKTPAaeitpRVMEALRMVQLetfaQRKPH---------QLSGGQQQRVAIARAVV-NKPrLLLLDEslSALD- 179
Cdd:COG4615 422 -LGLDGEADPA-----RARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLeDRP-ILVFDE--WAADq 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 180 --------YklrKQMQNELKAlqrkLGITFVFVTHDqEEALTMSDRIVVMRDGRIEQDGTPR 233
Cdd:COG4615 489 dpefrrvfY---TELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-230 |
5.70e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.74 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRiMLDNEDITHVPAENRYVNTVFQSYALFphmtvFEN 109
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VWAERSIAYVPQQAWIMNATVRGNILF-----FDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 vafglrmqktpaaEITPRVMEALRMVQLET-FAQ----------RKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PTZ00243 747 -------------EDAARLADAVRVSQLEAdLAQlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 179 DYKLRKQMQNELkALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 230
Cdd:PTZ00243 814 DAHVGERVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-235 |
9.83e-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: 76.14 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLR-LIAGLETVDsGRIMLDNEdITHVPAEnryvntvfqsyALFPHMTVFENVAFGL 114
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKGS-VAYVPQQ-----------AWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 RMQKtpaaEITPRVMEALRMV-QLE-------TFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQM 186
Cdd:TIGR00957 724 ALNE----KYYQQVLEACALLpDLEilpsgdrTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129089 187 QNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:TIGR00957 800 FEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-206 |
1.21e-14 |
|
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: 75.17 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNE-DITHVPAENRYVNTVFQSYALFPhMTVF 107
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVPQRPYMTLGTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFGLRMQKtpaaeitprVMEALRMVQLETFAQRK---------PHQLSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:TIGR00954 543 DMKRRGLSDKD---------LEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 16129089 179 DYKLRKQMQNelkaLQRKLGITFVFVTH 206
Cdd:TIGR00954 614 SVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-226 |
3.14e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.37 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 10 QPSSLSPLVQLA--GIRKCFDGKE-----VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGlETV-----DSGRIM-- 75
Cdd:TIGR00956 47 QPTFPNALLKILtrGFRKLKKFRDtktfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDgfhigVEGVITyd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 76 -LDNEDIT-HVPAENRYVNtvfQSYALFPHMTVFENVAFGLRMqKTPAAeitpRVM--------EALRMVQLETFAQRKP 145
Cdd:TIGR00956 126 gITPEEIKkHYRGDVVYNA---ETDVHFPHLTVGETLDFAARC-KTPQN----RPDgvsreeyaKHIADVYMATYGLSHT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 146 HQ----------LSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTHDQ--EEALT 213
Cdd:TIGR00956 198 RNtkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAYE 276
|
250
....*....|...
gi 16129089 214 MSDRIVVMRDGRI 226
Cdd:TIGR00956 277 LFDKVIVLYEGYQ 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-238 |
3.19e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIthvpAENRYVNTVFQS 97
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 YA---------LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRL 168
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129089 169 LLLDESLSALDYKLRKQ---MQNELKAlqRKLGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:NF033858 158 LILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-226 |
7.90e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-HVPA-----------ENRyvntvfQSYALFPHMT 105
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRdairagimlcpEDR------KAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRMQKTPAAEITPRVME---ALRMVQLETFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWEaenADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 179 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-207 |
2.20e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.12 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldnedithvpaenRYVNTVFQS 97
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------------EIGETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 98 Y------ALFPHMTVFENVAFGLRMQKTPAAEITPRVmealrMVQLETFA----QRKPHQLSGGQQQRVAIARAVVNKPR 167
Cdd:TIGR03719 389 YvdqsrdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16129089 168 LLLLDESLSALDYklrkqmqNELKALQRKL----GITFVfVTHD 207
Cdd:TIGR03719 464 VLLLDEPTNDLDV-------ETLRALEEALlnfaGCAVV-ISHD 499
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-188 |
2.57e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 67.97 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEF----LTLL--------GPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEnrYVNTVFQSYALFP 102
Cdd:PRK13541 6 QLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGLRMQKTpaAEITPrvmEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:PRK13541 84 EMTVFENLKFWSEIYNS--AETLY---AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
....*.
gi 16129089 183 RKQMQN 188
Cdd:PRK13541 159 RDLLNN 164
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-238 |
3.66e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 3 QSKKLNKQPsslsplVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLdnedit 82
Cdd:PRK15064 311 QDKKLHRNA------LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 83 hvpAENRYVNTVFQ-SYALFPH-MTVFENVAfglrmQKTPAAEITPRVMEAL-RMVQLETFAQRKPHQLSGGQQQRVAIA 159
Cdd:PRK15064 379 ---SENANIGYYAQdHAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 160 RAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQrklGiTFVFVTHDQEEALTMSDRIVVMRDGRIEQ-DGTpreiYEE 238
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGT----YEE 522
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-225 |
4.53e-13 |
|
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: 66.24 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNedithvpaenryvntvfqsyalfphmtvfenvafglrmqktpaa 122
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 123 eiTPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQ-----NELKALQRKL 197
Cdd:smart00382 38 --GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|...
gi 16129089 198 GITFVFVTHDQEEALTM-----SDRIVVMRDGR 225
Cdd:smart00382 116 NLTVILTTNDEKDLGPAllrrrFDRRIVLLLIL 148
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-272 |
6.70e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAG-LETVDSGRIMLDNEdITHVPAenryVNTVFQSyalfphmTVFENVAFGL 114
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-VAYVPQ----VSWIFNA-------TVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 -----RMQKTPAAEITPRVMEALRMVQLETFAQRKPHqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNe 189
Cdd:PLN03130 704 pfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD- 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 190 lKALQRKL-GITFVFVThDQEEALTMSDRIVVMRDGRIEQDGTpreiYEEpknLFVAGFIGEINMFNATVIERLDEQRVR 268
Cdd:PLN03130 782 -KCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----YEE---LSNNGPLFQKLMENAGKMEEYVEENGE 852
|
....
gi 16129089 269 ANVE 272
Cdd:PLN03130 853 EEDD 856
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-230 |
1.48e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLE--TVDSGRIMLDNEDITHVPAENRYVNTVFQSyalFPHMT 105
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMA---FQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQL---------------SGGQQQRVAIARAVVNKPRLLL 170
Cdd:PRK09580 89 EIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 171 LDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQE-EALTMSDRIVVMRDGRIEQDG 230
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
31-254 |
1.45e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.82 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 31 EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLET----VDSGRIMLDNEDITHVPAENRY------VNTVFQ--SY 98
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRklvghnVSMIFQepQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ALFPHmtvfENVAFGLrMQKTPAAEITPRVMEAL-----RMVQL---------ETFAQRKPHQLSGGQQQRVAIARAVVN 164
Cdd:PRK15093 101 CLDPS----ERVGRQL-MQNIPGWTYKGRWWQRFgwrkrRAIELlhrvgikdhKDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 165 KPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFV 244
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYT 255
|
250
....*....|
gi 16129089 245 AGFIGEINMF 254
Cdd:PRK15093 256 QALIRAIPDF 265
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-237 |
1.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-LETVDSGRIMLDNEdITHVPAenryVNTVFQSyalfphmTVFE 108
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-VAYVPQ----VSWIFNA-------TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRMQKT---PAAEITprvmeALRMvQLETFAQRKPHQL-------SGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PLN03232 698 NILFGSDFESErywRAIDVT-----ALQH-DLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 179 DYKLRKQ-----MQNELKalqrklGITFVFVThDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 237
Cdd:PLN03232 772 DAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-220 |
1.54e-11 |
|
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: 65.58 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDnEDITHVPaenRYVNTVFqsyalfpHMTVFENvafgLRMQK 118
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKP---QYISPDY-------DGTVEEF----LRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 TPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLG 198
Cdd:COG1245 427 TDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
170 180
....*....|....*....|....*.
gi 16129089 199 ITFVFVTHDqeeaLTM----SDRIVV 220
Cdd:COG1245 507 KTAMVVDHD----IYLidyiSDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-220 |
2.20e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDnEDITHVPaenRYVNTVFqsyalfpHMTVFENvafgLRMqk 118
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP---QYIKPDY-------DGTVEDL----LRS-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 tpaaeITPRVM------EALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 192
Cdd:PRK13409 424 -----ITDDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|..
gi 16129089 193 LQRKLGITFVFVTHDqeeaLTM----SDRIVV 220
Cdd:PRK13409 499 IAEEREATALVVDHD----IYMidyiSDRLMV 526
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-227 |
2.43e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDS--GRIMLDNE-----DITHvpAENRYVNTV 94
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD--SEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 95 FQSYALFPHMTVFENVAFGLRMQKTPA---AEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129089 172 DESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IE 227
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-229 |
4.65e-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: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 39 TINNGEFLTLLGPSGCGKTTVLRLIAGL-ETVDSGRIMLDNED-------------ITHVPaENRyvntvfQSYALFPHM 104
Cdd:TIGR02633 282 SLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPvdirnpaqairagIAMVP-EDR------KRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 105 TVFENV------AFGLRMQKTPAAEITPrVMEALRMVQLETFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:TIGR02633 355 GVGKNItlsvlkSFCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 178 LDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 229
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
38-222 |
5.08e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 38 LTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENrYVNTVFQSYAL---FPhmTVFENVAFGL 114
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN-LVAYVPQSEEVdwsFP--VLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 R-----MQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNE 189
Cdd:PRK15056 105 RyghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170 180 190
....*....|....*....|....*....|...
gi 16129089 190 LKALqRKLGITFVFVTHDQEEALTMSDRIVVMR 222
Cdd:PRK15056 185 LREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
40-240 |
5.41e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIT-HVP-----------AENRYVNTVFQSYALFPHMTVF 107
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPldavkkgmayiTESRRDNGFFPNFSIAQNMAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENV-------AFGL---RMQKTPAAEitPRVMEALRMVQLEtfaqRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PRK09700 366 RSLkdggykgAMGLfheVDEQRTAEN--QRELLALKCHSVN----QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 178 LD-------YKLRKQMQNElkalqrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 240
Cdd:PRK09700 440 IDvgakaeiYKVMRQLADD--------GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEE 501
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-238 |
7.82e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGLETVDsGRIMLDNEDITHVPAEN-RYVNTVF-QSYALFphmtvfe 108
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGLNIAKIGLHDlRFKITIIpQDPVLF------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 nvAFGLRMQKTPAAEITPR-VMEALRMVQLETFAQRKP----HQ-------LSGGQQQRVAIARAVVNKPRLLLLDESLS 176
Cdd:TIGR00957 1373 --SGSLRMNLDPFSQYSDEeVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129089 177 ALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGTPREIYEE 238
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-225 |
9.66e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 20 LAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDI---THVPAENRYVNTVFQ 96
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 97 SYALFPHMTVFENVAFGLRMQKTPAAEI------TPRVMEALrmvQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdTKAIFDEL---DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 171 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 225
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-199 |
1.10e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGK---EVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIML-DNEDITHVPAE--NRYV 91
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 92 NTVFQSYALFPHmTVFENVAFGLR----------------------------------------MQKTPAAEIT------ 125
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 126 -----PRVMEALRMVQLETFAQRKP-----------HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYK---LRKQM 186
Cdd:PTZ00265 542 qtikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKT 621
|
250
....*....|...
gi 16129089 187 QNELKALQRKLGI 199
Cdd:PTZ00265 622 INNLKGNENRITI 634
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-219 |
1.36e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDIthvpaenryVNTVFQSYALFPHMTVFENVAFGLRM 116
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI---------VARLQQDPPRNVEGTVYDFVAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 117 QktpaAEITPRVMEALRMV----------QLETFAQRKPHQ--------------------------LSGGQQQRVAIAR 160
Cdd:PRK11147 94 Q----AEYLKRYHDISHLVetdpseknlnELAKLQEQLDHHnlwqlenrinevlaqlgldpdaalssLSGGWLRKAALGR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 161 AVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIV 219
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIV 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-229 |
1.41e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKT-TVLRLIAGLETVDSGRIMLDNEDIT-------------HVPaENRyvntvfQSYALFPHMTVFE 108
Cdd:PRK13549 288 GEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKirnpqqaiaqgiaMVP-EDR------KRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVA------FGLRMQKTPAAEITpRVMEALRMVQLETFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD-- 179
Cdd:PRK13549 361 NITlaaldrFTGGSRIDDAAELK-TILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvg 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 180 --YKLRKQMqNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 229
Cdd:PRK13549 440 akYEIYKLI-NQLV----QQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-207 |
1.46e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMldnedithvPAENRYVNTVFQSYALFPHMTVFE 108
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGIKVGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 109 NVAFGLRMQK--------------TPAAEITP-------------------------RVMEALRMVQLETFAQRkphqLS 149
Cdd:TIGR03719 88 NVEEGVAEIKdaldrfneisakyaEPDADFDKlaaeqaelqeiidaadawdldsqleIAMDALRCPPWDADVTK----LS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129089 150 GGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHD 207
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPG-TVVAVTHD 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-273 |
2.12e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.67 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVlRLIAGLETVDSGR-------IMLDNEDITHVPAENRY 90
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*tWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 91 VNTVFQSyalfpHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLL 170
Cdd:NF000106 93 VR*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 171 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEpknlfVAGFIGE 250
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK-----VGGRTLQ 241
|
250 260
....*....|....*....|...
gi 16129089 251 INMFNATVIERLDEQRVRANVEG 273
Cdd:NF000106 242 IRPAHAAELDRMVGAIAQAGLDG 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-243 |
2.34e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHMtvfen 109
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGT----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 vafgLRMQKTPAAEIT-PRVMEALRMVQLETFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PLN03232 1326 ----VRFNIDPFSEHNdADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 178 LDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 243
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-211 |
5.24e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 16 PLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGletvD-----------------SGRIMLD- 77
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgysndltlfgrrrgSGETIWDi 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 78 NEDITHVPAE-------NRYVNTVFQSyALFPHMTVFENVAFGLRMqktpaaeitpRVMEALRMVQLETFAQRKP-HQLS 149
Cdd:PRK10938 335 KKHIGYVSSSlhldyrvSTSVRNVILS-GFFDSIGIYQAVSDRQQK----------LAQQWLDILGIDKRTADAPfHSLS 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 150 GGQQQRVAIARAVVNKPRLLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTHDQEEA 211
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLD------------PLNRQLVRRFVdvlisegetqllFVSHHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
46-226 |
7.85e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 46 LTLLGPSGCGKTTVLRLIAGLETVDSGrimldnedithvpaenryvnTVFQSYALfpHMTVF-ENVAFGLRMQKTP---A 121
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG--------------------TVFRSAKV--RMAVFsQHHVDGLDLSSNPllyM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 122 AEITPRVMEALRMVQLETF------AQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQR 195
Cdd:PLN03073 596 MRCFPGVPEQKLRAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG 675
|
170 180 190
....*....|....*....|....*....|.
gi 16129089 196 klGItfVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PLN03073 676 --GV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-224 |
1.18e-09 |
|
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: 58.71 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 26 CFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGlETVDSGRIMLDNEDITHVPaenryvntvfQSYALFPHmT 105
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-ELEPSEGKIKHSGRISFSS----------QFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENVAFGLRMQKTpaaeitpRVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:cd03291 114 IKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16129089 175 LSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDG 224
Cdd:cd03291 187 FGYLDVFTEKEIFEScvCKLMANK---TRILVTSKMEH-LKKADKILILHEG 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
43-179 |
2.42e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLET--VDSGRIMLDNEDIThvPAENRYVNTVFQSYALFPHMTVFENVAFGlrmqktp 120
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVREALRFS------- 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 121 aaeitprvmEALRMVQLEtfaQRKphqlsggqqqRVAIARAVVNKPRLLLLDESLSALD 179
Cdd:cd03232 104 ---------ALLRGLSVE---QRK----------RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-243 |
6.98e-09 |
|
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: 56.07 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 30 KEVIPQLDLTINNGEFLTLLGPSGCGKTTVLrlIAGLETVD--SGRIMLDNEDITHVPAEN--RYVNTVFQSYALFphmt 105
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHTlrSRLSIILQDPILF---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 vfenvAFGLRMQKTPAAEIT-PRVMEALRMVQLETFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDE 173
Cdd:cd03288 108 -----SGSIRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 174 SLSALDYKLRKQMQN-ELKALQRKlgiTFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLF 243
Cdd:cd03288 183 ATASIDMATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-179 |
9.36e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 22 GIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldnedithvpaenRYVNTVFQSY--- 98
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------------KIGETVKLAYvdq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 99 ---ALFPHMTVFENVAFGLRMQKTPAAEITPRVMealrmvqLETFA------QRKPHQLSGGQQQRVAIARAVVNKPRLL 169
Cdd:PRK11819 395 srdALDPNKTVWEEISGGLDIIKVGNREIPSRAY-------VGRFNfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 16129089 170 LLDESLSALD 179
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-224 |
4.59e-08 |
|
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: 55.30 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-LETVD-----SGRIMLDNEDITHVPAenryvntvfqsyalfp 102
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkikhSGRISFSPQTSWIMPG---------------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 hmTVFENVAFGLRMQKTpaaeitpRVMEALRMVQLETFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPRLLLL 171
Cdd:TIGR01271 502 --TIKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 172 DESLSALDYKLRKQMQNE--LKALQRKlgiTFVFVTHDQEEaLTMSDRIVVMRDG 224
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFESclCKLMSNK---TRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-179 |
5.45e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 27 FDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldneditHVPA--ENRYvntvFQSY--ALFP 102
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTklEVAY----FDQHraELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 103 HMTVFENVAFGlrmQKTpaAEITPRVMEALRMVQLETFAQRKPHQ----LSGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PRK11147 397 EKTVMDNLAEG---KQE--VMVNGRPRHVLGYLQDFLFHPKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
.
gi 16129089 179 D 179
Cdd:PRK11147 472 D 472
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-227 |
5.90e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 9 KQPSSL-SPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLdnedithvpAE 87
Cdd:PRK10636 303 RAPESLpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVFQsyalfpHMTVFenvafgLRMQKTP---AAEITPRVMEALRMVQLETFAQR------KPHQLSGGQQQRVAI 158
Cdd:PRK10636 374 GIKLGYFAQ------HQLEF------LRADESPlqhLARLAPQELEQKLRDYLGGFGFQgdkvteETRRFSGGEKARLVL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 159 ARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGRIE 227
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
48-207 |
7.09e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 48 LLGPSGCGKTTVLRLIAGLETVDSGRImldnedithVPAENRYVNTVFQSYALFPHMTVFENVAFGLRMQK--------- 118
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfnei 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 -----TPAAEitprvMEAL--RMVQLETF------------------AQRKPH------QLSGGQQQRVAIARAVVNKPR 167
Cdd:PRK11819 109 yaayaEPDAD-----FDALaaEQGELQEIidaadawdldsqleiamdALRCPPwdakvtKLSGGERRRVALCRLLLEKPD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16129089 168 LLLLDESlsaldyklrkqmQNELKA---------LQRKLGiTFVFVTHD 207
Cdd:PRK11819 184 MLLLDEP------------TNHLDAesvawleqfLHDYPG-TVVAVTHD 219
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-220 |
1.89e-07 |
|
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: 50.65 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPaenRYVNtvfqsyalfphmtvfenvafglrmqkt 119
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP---QYID--------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 120 paaeitprvmealrmvqletfaqrkphqLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGI 199
Cdd:cd03222 72 ----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 16129089 200 TFVFVTHDQEEALTMSDRIVV 220
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) ... |
43-253 |
2.33e-07 |
|
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: 51.60 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMlDNEDITHVPAENRyvNTVFQSYalfphmtvFENVAFG-LRMQKTPA 121
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFR--GSELQNY--------FTKLLEGdVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 122 -AEITPRVM------------------EALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKL 182
Cdd:cd03236 95 yVDLIPKAVkgkvgellkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 183 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRdgrieqdGTPRE--IYEEPK------NLFVAGFIGEINM 253
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY-------GEPGAygVVTLPKsvregiNEFLDGYLPTENM 245
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-226 |
3.67e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLD---------NEDITH----VPAENR----YVNTVFQSYALFPHMT 105
Cdd:PRK10982 274 GEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHgkkinnhnaNEAINHgfalVTEERRstgiYAYLDIGFNSLISNIR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 106 VFENvAFGL----RMQKTpaaeiTPRVMEALRmvqLETFAQRKP-HQLSGGQQQRVAIARAVVNKPRLLLLDESLSALD- 179
Cdd:PRK10982 354 NYKN-KVGLldnsRMKSD-----TQWVIDSMR---VKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDv 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16129089 180 ------YKLRKQMQNELKalqrklGItfVFVTHDQEEALTMSDRIVVMRDGRI 226
Cdd:PRK10982 425 gakfeiYQLIAELAKKDK------GI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
36-267 |
4.96e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRImldneDITHVPAenryvnTVFQSYALFPHMTVFENVAF-GL 114
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAA------LIAISSGLNGQLTGIENIELkGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 RM--QKTPAAEITPRVMEalrMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKA 192
Cdd:PRK13545 112 MMglTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129089 193 LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNlfvagFIGEINMFNATVIERLDEQRV 267
Cdd:PRK13545 189 FKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE-----FLKKYNQMSVEERKDFREEQI 257
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-222 |
1.87e-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: 47.35 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 35 QLDLTINNGEFLTLLGPSGCGKTTVLRLIAgletvdsgrimldnedithvpaenryvntvfqsYALFPHMTVFENVAFGL 114
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 115 RMQKTPAAEITPRVMEalrmvqletfaqrkpHQLSGGQQQRVAIARAVVN---KPR-LLLLDESLSALDyklrkqMQNEL 190
Cdd:cd03227 60 AGCIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslKPRpLYILDEIDRGLD------PRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 16129089 191 KAL-----QRKLGITFVFVTHDQEEALtMSDRIVVMR 222
Cdd:cd03227 119 ALAeaileHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-179 |
2.57e-06 |
|
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: 49.52 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDsGRIMLDNedithVPAENRYVNTVFQSYALFPHMTVF 107
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG-----VSWNSVTLQTWRKAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFglRMQKTPAAEITP----RVME--ALRMVqLETFAQRKPHQ-------LSGGQQQRVAIARAVVNKPRLLLLDES 174
Cdd:TIGR01271 1304 FSGTF--RKNLDPYEQWSDeeiwKVAEevGLKSV-IEQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
....*
gi 16129089 175 LSALD 179
Cdd:TIGR01271 1381 SAHLD 1385
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
43-224 |
3.21e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLET--VDSGRIMLDN---EDITHvpaeNRYVNTVFQSYALFPHMTVFENVAFGLRM- 116
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgVITGGDRLVNgrpLDSSF----QRSIGYVQQQDLHLPTSTVRESLRFSAYLr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 117 --QKTPAAEITPRVMEALRMVQLETFAQR---KPHQ-LSGGQQQRVAIARAVVNKPRLLL-LDESLSALDyklrKQMQNE 189
Cdd:TIGR00956 865 qpKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD----SQTAWS 940
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129089 190 LKALQRKL---GITFVFVTHdQEEALTMS--DRIVVMRDG 224
Cdd:TIGR00956 941 ICKLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-235 |
4.80e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 32 VIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHMTVFEN 109
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 110 VAFGlrmqKTPAAEItprvMEALRMVQLETFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLDESLSAL 178
Cdd:PLN03130 1334 DPFN----EHNDADL----WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129089 179 DYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 235
Cdd:PLN03130 1406 DVRtdalIQKTIREEFKS------CTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
43-221 |
5.17e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGletvdsgrIMLDNEDITHVPAE-----NRYVNTVFQSYalfphmtvFENVAFG-LR- 115
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSG--------ELIPNLGDYEEEPSwdevlKRFRGTELQNY--------FKKLYNGeIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 MQKTPAAEITPRVM-----EALRMV-------------QLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSA 177
Cdd:PRK13409 163 VHKPQYVDLIPKVFkgkvrELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16129089 178 LDYKLRKQMQNELKALQRklGITFVFVTHDqeeaLT----MSDRIVVM 221
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-238 |
5.78e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 37 DLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAE--NRYVNTVFQ---SYALFPhmtvfENVA 111
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlQKLVSDEWQrnnTDMLSP-----GEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 112 FGlrmqKTpAAEI-------TPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRK 184
Cdd:PRK10938 98 TG----RT-TAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129089 185 QMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 238
Cdd:PRK10938 173 QLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-221 |
6.16e-06 |
|
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: 48.24 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 43 GEFLTLLGPSGCGKTTVLRLIAGLETVDSGRI--MLDNEDIThvpaeNRYVNTVFQSYalfphmtvFENVAFG-LRM-QK 118
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYdeEPSWDEVL-----KRFRGTELQDY--------FKKLANGeIKVaHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 119 TPAAEITPRV------------------MEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDY 180
Cdd:COG1245 166 PQYVDLIPKVfkgtvrellekvdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16129089 181 KLRKQMQNELKALQRKlGITFVFVTHDqeeaLT----MSDRIVVM 221
Cdd:COG1245 246 YQRLNVARLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-243 |
1.76e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 40 INNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAEN--RYVNTVFQSYALFPHmTVFENVafglrmq 117
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNV------- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 118 kTPAAEITP-RVMEALRMVQL-----------ETFAQRKPHQLSGGQQQRVAIARAVVNKPR-LLLLDESLSALDYKLRK 184
Cdd:PTZ00243 1405 -DPFLEASSaEVWAALELVGLrervasesegiDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDR 1483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 185 QMQNE-LKALQRKLGITFVFVTHdqeeALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 243
Cdd:PTZ00243 1484 QIQATvMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
36-266 |
3.45e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 36 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEdithvpaenryVNTVFQSYALFPHMTVFENVAFGLR 115
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 116 MQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQR 195
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129089 196 KlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI---YEEPKNLFVAGFIGEINMFNatviERLDEQR 266
Cdd:PRK13546 192 Q-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDFKKKSKAEQKEFR----NKLDESR 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
88-242 |
3.82e-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: 45.77 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 88 NRYVNTVF---QSYALFPHMTVFENVAF----GLRMQKTPAA-----EITPRVmEALRMVQLETFA-QRKPHQLSGGQQQ 154
Cdd:TIGR00630 417 KPEALAVTvggKSIADVSELSIREAHEFfnqlTLTPEEKKIAeevlkEIRERL-GFLIDVGLDYLSlSRAAGTLSGGEAQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 155 RVAIARAV------VnkprLLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM------R 222
Cdd:TIGR00630 496 RIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIgpgageH 569
|
170 180
....*....|....*....|
gi 16129089 223 DGRIEQDGTPREIYEEPKNL 242
Cdd:TIGR00630 570 GGEVVASGTPEEILANPDSL 589
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-228 |
5.32e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 28 DGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDsGRIMLDNEDITHVPAENRYvntvfQSYALFPHMTVF 107
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 108 ENVAFglRMQKTP----AAEITPRVMEAlrmVQLETFAQRKPHQL-----------SGGQQQRVAIARAVVNKPRLLLLD 172
Cdd:cd03289 89 FSGTF--RKNLDPygkwSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 173 ESLSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQ 228
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
148-226 |
8.51e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 148 LSGGQQQRVAIARAVVNKPRLLLLDESLSALD-------YKLRKQMQNELKALqrklgitfVFVTHDQEEALTMSDRIVV 220
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyeiYTIINELAAEGKGV--------IVISSELPELLGMCDRIYV 476
|
....*.
gi 16129089 221 MRDGRI 226
Cdd:NF040905 477 MNEGRI 482
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
18-231 |
8.97e-05 |
|
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: 42.98 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 18 VQLAGIRkCFDGKEVIpqldltinngEF---LTLL-GPSGCGKTTvlrLIAGLETVDSGRIMLDNEDITHVP-----AEN 88
Cdd:cd03240 4 LSIRNIR-SFHERSEI----------EFfspLTLIvGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPklireGEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 89 R-YVNTVFQS-----YALFPHMTVFENVAFglrmqktpaaeitprvmeaLRMVQLETFAQRKPHQLSGGQQQ------RV 156
Cdd:cd03240 70 RaQVKLAFENangkkYTITRSLAILENVIF-------------------CHQGESNWPLLDMRGRCSGGEKVlasliiRL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129089 157 AIARAVVNKPRLLLLDESLSALD-YKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVvmrdgRIEQDGT 231
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY-----RVEKDGR 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-221 |
9.36e-05 |
|
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: 42.70 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 33 IPQLDLTINNGEFLTLLGPSGCGKTTVLRliAGLETVdsgrimldnedithvpAENRYVNTvfqsyalfphmtvfenvaf 112
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS----------------GKARLISF------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 113 glrmqkTPAAEITPRVMealrMVQLETFAQ---------RKPHQLSGGQQQRVAIAR--AVVNKPRLLLLDESLSALDYK 181
Cdd:cd03238 54 ------LPKFSRNKLIF----IDQLQFLIDvglgyltlgQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16129089 182 LRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM 221
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
50-82 |
1.29e-04 |
|
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: 41.70 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|....*.
gi 16129089 50 GPSGCGKTTVLRLIA---GLETVDSGRImlDNEDIT 82
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGI--RTEEVG 39
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
292-372 |
4.36e-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: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 292 VLLRPEDLRVEEInddnhAEGLIGYVRERNYKGMTLESVVELENGKMVMVSEFFNEDDPdfdHSLDQKMAINWVESWEVV 371
Cdd:pfam08402 1 LAIRPEKIRLAAA-----ANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHV 72
|
.
gi 16129089 372 L 372
Cdd:pfam08402 73 L 73
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-209 |
1.36e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 29 GKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIA-----GL-----------ETVDSGRIMLD---NEDITHVPAENR 89
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveqEVVGDDTTALQcvlNTDIERTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129089 90 YVNTVFQSYAL-FPHMTVFENVAFGLRMQKTPA----AEITPRvMEALRMVQLETFA--------------QRKPHQLSG 150
Cdd:PLN03073 269 EAQLVAQQRELeFETETGKGKGANKDGVDKDAVsqrlEEIYKR-LELIDAYTAEARAasilaglsftpemqVKATKTFSG 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129089 151 GQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHDQE 209
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHARE 402
|
|
| |
