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Conserved domains on  [gi|1003869982|gb|KXY64124|]
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phosphonate ABC transporter ATP-binding protein [Bacillus cereus]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11496526)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including ions, such as Chromobacterium violaceum sulfate/thiosulfate import ATP-binding protein CysA 2 and Sinorhizobium meliloti Fe(3+) ions import ATP-binding protein FbpC 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-328 0e+00

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: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINF 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 241 FSKNNEEH-------------------------AIRPEHVTV----VQNNGMKTIVESMEFRGSVYRTEVRVIDEKTHly 291
Cdd:TIGR03265 241 LPGTRGGGsrarvggltlacapglaqpgasvrlAVRPEDIRVspagNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQ-- 318

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1003869982 292 neKIVVDILASEVEKTAIRKGQPIQISFSENHMLSYG 328
Cdd:TIGR03265 319 --ALVADVSASEVERLGIRAGQPIWIELPAERLRAFA 353
 
Name Accession Description Interval E-value
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-328 0e+00

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: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINF 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 241 FSKNNEEH-------------------------AIRPEHVTV----VQNNGMKTIVESMEFRGSVYRTEVRVIDEKTHly 291
Cdd:TIGR03265 241 LPGTRGGGsrarvggltlacapglaqpgasvrlAVRPEDIRVspagNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQ-- 318

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1003869982 292 neKIVVDILASEVEKTAIRKGQPIQISFSENHMLSYG 328
Cdd:TIGR03265 319 --ALVADVSASEVERLGIRAGQPIWIELPAERLRAFA 353
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-324 4.83e-175

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 489.22  E-value: 4.83e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINF 240
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 241 FS----KNNEEH------------------------AIRPEHVTVVQN---NGMKTIVESMEFRGSVYRTEVRVIDekth 289
Cdd:COG3842   242 LPgtvlGDEGGGvrtggrtlevpadaglaaggpvtvAIRPEDIRLSPEgpeNGLPGTVEDVVFLGSHVRYRVRLGD---- 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1003869982 290 lyNEKIVVDILASEVEktAIRKGQPIQISFSENHM 324
Cdd:COG3842   318 --GQELVVRVPNRAAL--PLEPGDRVGLSWDPEDV 348
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.32e-127

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: 364.25  E-value: 1.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-309 8.57e-115

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 336.92  E-value: 8.57e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFSkn 244
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD-- 252

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 245 neehairpehVTVVQNNGMKTIVESMEFRGSVYRTEVRV-IDEKTH--LYNEKIVVDILASEVEKTAI 309
Cdd:PRK09452  253 ----------ATVIERLDEQRVRANVEGRECNIYVNFAVePGQKLHvlLRPEDLRVEEINDDEHAEGL 310
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
5-279 4.11e-92

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 278.11  E-value: 4.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFskn 244
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENII--- 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1003869982 245 nEEHAIRPEHVTVVQNNGMKtIVESMEFRGSVYRT 279
Cdd:NF040840  238 -EGVAEKGGEGTILDTGNIK-IELPEEKKGKVRIG 270
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
5-208 2.28e-51

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 169.51  E-value: 2.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFT----ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-----K 75
Cdd:NF038007    2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkiilR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNF-GMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:NF038007   82 RELiGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHdQEEALTMADKIVVM 208
Cdd:NF038007  162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINM 213
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-163 4.12e-51

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: 166.28  E-value: 4.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNLTALENI 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKAKKYGKAEVKEKALSALELVDLLNVKD----KYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-208 8.99e-29

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 109.63  E-value: 8.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPgkrnfgmvfQSYAL---FPn 90
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVP---------QRSEVpdsLP- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYG--------KAEVkEKALSALELVDLLNvkdKYPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:NF040873   72 LTVRDLVAMGRWARRGLwrrltrddRAAV-DDALERVGLADLAG---RQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 163 SALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTmADKIVVM 208
Cdd:NF040873  148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-222 5.84e-25

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 5.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   8 QHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI-----AVNGKDITAlppgKRNFGMVF 82
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT----RRRVGYMS 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEygLKAKKYG--KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:NF033858  346 QAFSLYGELTVRQNLE--LHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMnHA-EIMQIGTPEEI 222
Cdd:NF033858  424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLM-HAgRVLASDTPAAL 484
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-207 6.18e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 6.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT--GSIAVNG-----KDITAlppgKRN 77
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD----SEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVF--QSYALFPNLTALENIEYGLKAKKYG---KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALS 152
Cdd:NF040905   78 LGIVIihQELALIPYLSIAENIFLGNERAKRGvidWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVV 207
Cdd:NF040905  158 VKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITV 211
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
18-225 2.18e-14

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 74.01  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI------TALPP---------GKrNfgmvf 82
Cdd:NF033858   15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCPriaympqglGK-N----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 qsyaLFPNLTALENIE-----YGLkakkyGKAEVKEKALSALELVDLLNVKDKyPA-QMSGGQQQRVALARALALSPDIL 156
Cdd:NF033858   89 ----LYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 157 LLDE------PLSaldakvreklRREMRDL-----QEKVGVTTIMVTHDQEEALTMaDKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:NF033858  159 ILDEpttgvdPLS----------RRQFWELidrirAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-213 1.52e-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: 67.01  E-value: 1.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   29 KNEFVCLLGPSGCGKTTLLRILAG-LEEATTGSIAVNGkditalppgkrnfgmvfqsyalfpnltalenieyglkakkyg 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------ 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  108 kaevkEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRD-----LQE 182
Cdd:smart00382  39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1003869982  183 KVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
108-222 4.74e-10

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 108 KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVT 187
Cdd:NF000106  118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1003869982 188 TIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:NF000106  197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-213 3.09e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.55  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAT--TGSIAVNGKDIT------ALPPG----------------- 74
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDvstvsdAIDAGlayvtedrkgyglnlid 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 --KRNFGMvfqsyalfPNLTAL-------ENIEYGLkAKKYgKAEVKEKALSALELVdllnvkdkypAQMSGGQQQRVAL 145
Cdd:NF040905  356 diKRNITL--------ANLGKVsrrgvidENEEIKV-AEEY-RKKMNIKTPSVFQKV----------GNLSGGNQQKVVL 415

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 146 ARALALSPDILLLDEPLSALD--AKVreklrrE----MRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:NF040905  416 SKWLFTDPDVLILDEPTRGIDvgAKY------EiytiINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
 
Name Accession Description Interval E-value
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-328 0e+00

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: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR03265  81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINF 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 241 FSKNNEEH-------------------------AIRPEHVTV----VQNNGMKTIVESMEFRGSVYRTEVRVIDEKTHly 291
Cdd:TIGR03265 241 LPGTRGGGsrarvggltlacapglaqpgasvrlAVRPEDIRVspagNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQ-- 318

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1003869982 292 neKIVVDILASEVEKTAIRKGQPIQISFSENHMLSYG 328
Cdd:TIGR03265 319 --ALVADVSASEVERLGIRAGQPIWIELPAERLRAFA 353
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-324 4.83e-175

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 489.22  E-value: 4.83e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINF 240
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 241 FS----KNNEEH------------------------AIRPEHVTVVQN---NGMKTIVESMEFRGSVYRTEVRVIDekth 289
Cdd:COG3842   242 LPgtvlGDEGGGvrtggrtlevpadaglaaggpvtvAIRPEDIRLSPEgpeNGLPGTVEDVVFLGSHVRYRVRLGD---- 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1003869982 290 lyNEKIVVDILASEVEktAIRKGQPIQISFSENHM 324
Cdd:COG3842   318 --GQELVVRVPNRAAL--PLEPGDRVGLSWDPEDV 348
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-324 8.98e-151

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 427.57  E-value: 8.98e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEyLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:COG3839     1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG3839    80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS--I 238
Cdd:COG3839   160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 239 NFFSKNNEEH-------------------------AIRPEHVTVVQ--NNGMKTIVESMEFRGSVYRTEVRVIDEkthly 291
Cdd:COG3839   240 NLLPGTVEGGgvrlggvrlplpaalaaaaggevtlGIRPEHLRLADegDGGLEATVEVVEPLGSETLVHVRLGGQ----- 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1003869982 292 nekivvDILASEVEKTAIRKGQPIQISFSENHM 324
Cdd:COG3839   315 ------ELVARVPGDTRLRPGDTVRLAFDPERL 341
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 1-319 1.51e-144

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 411.46  E-value: 1.51e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSeyLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-TALPPGKRNFG 79
Cdd:COG1118     1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:COG1118    79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 160 EPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSIN 239
Cdd:COG1118   159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 240 FFS---------------------KNNEEHA-IRPEHVTVV----QNNGMKTIVESMEFRGSVYRTEVRVIDEKTHLyne 293
Cdd:COG1118   239 VLRgrviggqleadgltlpvaeplPDGPAVAgVRPHDIEVSrepeGENTFPATVARVSELGPEVRVELKLEDGEGQP--- 315

                         330       340
                  ....*....|....*....|....*.
gi 1003869982 294 kIVVDILASEVEKTAIRKGQPIQISF 319
Cdd:COG1118   316 -LEAEVTKEAWAELGLAPGDPVYLRP 340
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.32e-127

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: 364.25  E-value: 1.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 5-217 4.87e-117

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: 336.80  E-value: 4.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 7-237 6.96e-115

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: 332.38  E-value: 6.96e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYA 86
Cdd:cd03296     5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENIEYGLKAKKYG----KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:cd03296    85 LFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 163 SALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS 237
Cdd:cd03296   165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-309 8.57e-115

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 336.92  E-value: 8.57e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFSkn 244
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD-- 252

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 245 neehairpehVTVVQNNGMKTIVESMEFRGSVYRTEVRV-IDEKTH--LYNEKIVVDILASEVEKTAI 309
Cdd:PRK09452  253 ----------ATVIERLDEQRVRANVEGRECNIYVNFAVePGQKLHvlLRPEDLRVEEINDDEHAEGL 310
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-233 5.78e-109

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 317.80  E-value: 5.78e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSE---YLSIQHIQKQF----DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlPP 73
Cdd:COG1116     1 MSAaapALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 GKRnfGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSP 153
Cdd:COG1116    80 PDR--GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 154 DILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNH-----AEIMQIGTPeeiyqRPAN 228
Cdd:COG1116   158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpgriVEEIDVDLP-----RPRD 232


                  ....*
gi 1003869982 229 PFVAD 233
Cdd:COG1116   233 RELRT 237
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 7-239 3.32e-108

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 315.20  E-value: 3.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYA 86
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:TIGR00968  83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 167 AKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSIN 239
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 5-217 6.22e-105

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: 306.10  E-value: 6.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-248 1.40e-104

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: 309.42  E-value: 1.40e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  35 LLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEK 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 115 ALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHD 194
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 195 QEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFSKNNEEH 248
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIER 214
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 7-290 2.14e-102

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 302.78  E-value: 2.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQ 83
Cdd:COG1125     4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDL--LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:COG1125    84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS---I 238
Cdd:COG1125   164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAdrgL 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 239 NFFSKNNEEHAIRPEHVTVVQNNGMKTIVESMEFRGsvyRTEVRVIDEKTHL 290
Cdd:COG1125   244 RRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERG---VDWLLVVDEDGRP 292
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 5-209 1.20e-101

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: 297.85  E-value: 1.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGkrnFGM 80
Cdd:cd03293     1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMN 209
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-266 2.55e-101

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 302.02  E-value: 2.55e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   4 YLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQ 83
Cdd:PRK11432    6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK11432   86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFSK 243
Cdd:PRK11432  166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1003869982 244 N--------NEEHAIRPEHVTVVQNNGMKTI 266
Cdd:PRK11432  246 TlsgdyvdiYGYRLPRPAAFAFNLPDGECTV 276
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
5-271 1.88e-98

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 294.83  E-value: 1.88e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDA-FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQ 83
Cdd:PRK11650    4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVK---EKALSALELVDLLnvkDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGMPKAEIEervAEAARILELEPLL---DRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS--I 238
Cdd:PRK11650  161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaM 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 239 NFFS-KNNEEHA---------------------------IRPEHVTVVQNN-GMKTIVESME 271
Cdd:PRK11650  241 NLLDgRVSADGAafelaggialplgggyrqyagrkltlgIRPEHIALSSAEgGVPLTVDTVE 302
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1-242 2.93e-98

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 294.30  E-value: 2.93e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSeyLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGM 80
Cdd:PRK10851    1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKA----KKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDIL 156
Cdd:PRK10851   79 VFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 157 LLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:PRK10851  159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238


                  ....*.
gi 1003869982 237 SINFFS 242
Cdd:PRK10851  239 EVNRLQ 244
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-241 4.28e-97

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 292.12  E-value: 4.28e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK11607  100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFF 241
Cdd:PRK11607  180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 5-237 1.56e-95

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: 283.04  E-value: 1.56e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMV 81
Cdd:cd03295     1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDL--LNVKDKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 160 EPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS 237
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 5-238 4.30e-94

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 279.19  E-value: 4.30e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlpPGK------RNF 78
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD--SKKdinklrRKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYGL-KAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILL 157
Cdd:COG1126    80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 158 LDEPLSALDAK-VREKLrREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:COG1126   160 FDEPTSALDPElVGEVL-DVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237


                  ..
gi 1003869982 237 SI 238
Cdd:COG1126   238 KV 239
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 5-236 1.73e-92

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: 275.37  E-value: 1.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03299     1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
5-279 4.11e-92

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 278.11  E-value: 4.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:NF040840    2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFskn 244
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENII--- 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1003869982 245 nEEHAIRPEHVTVVQNNGMKtIVESMEFRGSVYRT 279
Cdd:NF040840  238 -EGVAEKGGEGTILDTGNIK-IELPEEKKGKVRIG 270
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 10-235 1.05e-89

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: 269.51  E-value: 1.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG------KRNFGMVFQ 83
Cdd:cd03294    30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03294   110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFI 235
Cdd:cd03294   190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
6-263 9.66e-89

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 270.36  E-value: 9.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSY 85
Cdd:PRK11000    5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:PRK11000   85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 166 DAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS--INFFSK 243
Cdd:PRK11000  165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSpkMNFLPV 244

                         250       260
                  ....*....|....*....|
gi 1003869982 244 nnEEHAIRPEHVTVVQNNGM 263
Cdd:PRK11000  245 --KVTATAIEQVQVELPNRQ 262
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-235 3.28e-87

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: 261.84  E-value: 3.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK----- 75
Cdd:COG1127     2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNFGMVFQSYALFPNLTALENIEYGLKA-KKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:COG1127    82 RRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPaNPFVADF 234
Cdd:COG1127   162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240


                  .
gi 1003869982 235 I 235
Cdd:COG1127   241 L 241
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-208 1.11e-86

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 259.98  E-value: 1.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR 76
Cdd:COG1136     1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 ------NFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALA 150
Cdd:COG1136    81 arlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDqEEALTMADKIVVM 208
Cdd:COG1136   161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL 217
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 5-229 1.17e-82

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 259.45  E-value: 1.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-----DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK---- 75
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 -RNFGMVFQ--SYALFPNLTALENIEYGLKA-KKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALA 150
Cdd:COG1123   341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANP 229
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 5-213 1.22e-82

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: 249.33  E-value: 1.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDA----FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR---- 76
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 --NFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:cd03255    81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALtMADKIVVMNHAEI 213
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 19-333 1.53e-81

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: 251.70  E-value: 1.53e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP------GKRNFGMVFQSYALFPNLT 92
Cdd:TIGR01186   8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:TIGR01186  88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 173 LRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSINFFSKNNEEHAIRP 252
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFDAERIAQR 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 253 EHVTVVQNNGMKTIVESMEF-------------RGSVYRTEVRVIDEKTHLYNEKIVVDILASEVekTAIRKGQPIQISF 319
Cdd:TIGR01186 248 MNTGPITKTADKGPRSALQLmrdervdslyvvdRQNKLVGVVDVESIKQARKKAQGLQDVLIDDI--YTVDAGTLLRETV 325

                         330
                  ....*....|....
gi 1003869982 320 SenHMLSYGKKVVV 333
Cdd:TIGR01186 326 R--KVLKAGIKVPV 337
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 5-212 5.10e-78

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: 236.31  E-value: 5.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAL----PPGKRNFGM 80
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLkakkygkaevkekalsalelvdllnvkdkypaqmSGGQQQRVALARALALSPDILLLDE 160
Cdd:cd03229    81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAE 212
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 5-234 1.14e-77

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: 237.40  E-value: 1.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNFG 79
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENIEYGLKAK-KYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIyQRPANPFVADF 234
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-225 6.99e-77

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 235.34  E-value: 6.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQ 83
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 5-213 7.35e-77

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: 234.73  E-value: 7.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG----KRNFGM 80
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGL-KAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 160 EPLSALDAK-VREKLrREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03262   161 EPTSALDPElVGEVL-DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 15-226 3.36e-75

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: 231.07  E-value: 3.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQS--YALFpN 90
Cdd:COG1122    12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:COG1122    91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 171 EKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:COG1122   171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 5-238 3.90e-74

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: 228.92  E-value: 3.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF----DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNF 78
Cdd:COG1124     2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSY--ALFPNLTALENIEYGLKAkkYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRI--HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 156 LLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFI 235
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELL 239


                  ...
gi 1003869982 236 GSI 238
Cdd:COG1124   240 AAS 242
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-238 1.16e-73

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 230.73  E-value: 1.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK----- 75
Cdd:COG1135     2 IELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 156 LLLDEPLSALDAK----VREKLrremRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFV 231
Cdd:COG1135   162 LLCDEATSALDPEttrsILDLL----KDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237


                  ....*..
gi 1003869982 232 ADFIGSI 238
Cdd:COG1135   238 RRFLPTV 244
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-208 3.60e-71

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 221.66  E-value: 3.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEyLSIQHIQKQFDAF----TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlPPGKR 76
Cdd:COG4525     1 MSM-LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 nfGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDIL 156
Cdd:COG4525    79 --GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 157 LLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:COG4525   157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 10-217 2.04e-70

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: 218.32  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTAlkDISFTVKKnEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG-------KDITaLPPGKRNFGMVF 82
Cdd:cd03297     6 IEKRLPDFTL--KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQQRKIGLVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEYGLKAKKYGKAEVKEKALsaLELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:cd03297    82 QQYALFPHLNVRENLAFGLKRKRNREDRISVDEL--LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 163 SALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03297   160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 5-226 2.44e-70

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: 218.60  E-value: 2.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK----- 75
Cdd:cd03258     2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 156 LLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
5-236 6.05e-70

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 217.70  E-value: 6.05e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTalKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:COG3840     2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAK-KYGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG3840    80 NNLFPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 164 ALDAkvreKLRREM----RDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIG 236
Cdd:COG3840   159 ALDP----ALRQEMldlvDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-213 4.74e-69

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 214.92  E-value: 4.74e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNF 78
Cdd:COG2884     2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 159 DEPLSALDAKVREKLrreMRDLQE--KVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:COG2884   162 DEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-217 5.20e-69

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: 215.06  E-value: 5.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN--- 77
Cdd:cd03257     2 LEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 --FGMVFQSY--ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLN---VKDKYPAQMSGGQQQRVALARALA 150
Cdd:cd03257    82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 9-227 6.67e-69

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 219.20  E-value: 6.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   9 HIQKQFDAFTaLkDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK---DITA---LPPGKRNFGMVF 82
Cdd:COG4148     6 DFRLRRGGFT-L-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRRRIGYVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEYGLKakkygKAEVKEKALSALELVDLLNVK---DKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:COG4148    84 QEARLFPHLSVRGNLLYGRK-----RAPRAERRISFDEVVELLGIGhllDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 160 EPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:COG4148   159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-227 2.55e-68

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: 222.09  E-value: 2.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQF--DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAT---TGSIAVNGKDITALPPGK 75
Cdd:COG1123     1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 R--NFGMVFQS--YALFPnLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALAL 151
Cdd:COG1123    81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 152 SPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 19-210 5.07e-68

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: 211.94  E-value: 5.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQsyalFP-----NL 91
Cdd:cd03225    16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ----NPddqffGP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVRE 171
Cdd:cd03225    92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1003869982 172 KLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNH 210
Cdd:cd03225   172 ELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 5-222 1.56e-67

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 211.84  E-value: 1.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNF 78
Cdd:COG3638     3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYG-------LKA--KKYGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSllGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG3638   162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 5-222 4.15e-67

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: 211.06  E-value: 4.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVF 82
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEYG----LKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:COG1120    82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG1120   162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 5-229 1.56e-65

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: 209.14  E-value: 1.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEA---TTGSIAVNGKDITALPP---- 73
Cdd:COG0444     2 LEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 ---GKRnFGMVFQ-SY-ALFPNLTALENIEYGLKA-KKYGKAEVKEKALSALELVDLLN---VKDKYPAQMSGGQQQRVA 144
Cdd:COG0444    82 kirGRE-IQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 145 LARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:COG0444   161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                  ....*
gi 1003869982 225 RPANP 229
Cdd:COG0444   241 NPRHP 245
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 16-226 1.86e-65

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 207.69  E-value: 1.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  16 AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA-----LPPGKRNFGMVFQ--SYALF 88
Cdd:TIGR04521  17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDLRKKVGLVFQfpEHQLF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  89 PNlTALENIEYGLKAKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:TIGR04521  97 EE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 168 KVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 5-215 2.18e-65

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: 205.75  E-value: 2.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD----AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR---- 76
Cdd:COG4181     9 IELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 --NFGMVFQSYALFPNLTALENIeyGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:COG4181    89 arHVGFVFQSFQLLPTLTALENV--MLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALtMADKIVVMNHAEIMQ 215
Cdd:COG4181   167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVE 226
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
8-235 4.63e-65

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 205.33  E-value: 4.63e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   8 QHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNF----GMVFQ 83
Cdd:PRK09493    5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYG-LKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:PRK09493   85 QFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 163 SALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFI 235
Cdd:PRK09493  165 SALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 5-222 2.57e-64

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: 203.18  E-value: 2.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEA-----TTGSIAVNGKDITALPPG----K 75
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlelR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNFGMVFQSYALFPnLTALENIEYGLKAKKY-GKAEVKEKALSALELVDLL-NVKDKYPA-QMSGGQQQRVALARALALS 152
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRLHAlGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 5-224 6.60e-64

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: 202.41  E-value: 6.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNF 78
Cdd:cd03256     1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYGLKAKK---------YGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 5-227 2.44e-63

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: 200.74  E-value: 2.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN---FGMV 81
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKK----------YGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALAL 151
Cdd:cd03219    81 FQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 152 SPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 5-222 2.63e-63

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: 201.42  E-value: 2.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN-FGMV-- 81
Cdd:COG0411     5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArLGIArt 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIE---------------YGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALA 146
Cdd:COG0411    85 FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 147 RALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG0411   165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
5-213 2.27e-62

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 197.35  E-value: 2.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVF 82
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNlTALENIEYGLKAKKygKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:COG4619    81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:COG4619   158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 5-248 6.71e-62

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: 197.39  E-value: 6.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQ 83
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG4555    82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIgsINFFSK 243
Cdd:COG4555   162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF--VALIGS 238


                  ....*
gi 1003869982 244 NNEEH 248
Cdd:COG4555   239 EEGEA 243
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 20-226 2.93e-61

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: 195.38  E-value: 2.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRnfgMVFQSYALFPNLTALENIEY 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 100 GLKA--KKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREM 177
Cdd:TIGR01184  78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003869982 178 RDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI-YQRP 226
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 5-213 1.38e-60

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: 191.46  E-value: 1.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQ 83
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYglkakkygkaevkekalsalelvdllnvkdkypaqmSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03230    81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
5-237 1.02e-59

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 192.32  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDItALPPGKR-------- 76
Cdd:COG4598     9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRDgelvpadr 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 --------NFGMVFQSYALFPNLTALEN-IEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALAR 147
Cdd:COG4598    88 rqlqrirtRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 148 ALALSPDILLLDEPLSALDAK-VREKLrREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:COG4598   168 ALAMEPEVMLFDEPTSALDPElVGEVL-KVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245

                         250
                  ....*....|.
gi 1003869982 227 ANPFVADFIGS 237
Cdd:COG4598   246 KSERLRQFLSS 256
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-222 2.01e-59

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 191.07  E-value: 2.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlppGKRNFGM 80
Cdd:COG1121     3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYAL---FPnLTALENIEYGLKAKK-----YGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALS 152
Cdd:COG1121    80 VPQRAEVdwdFP-ITVRDVVLMGRYGRRglfrrPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHaEIMQIGTPEEI 222
Cdd:COG1121   158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEV 225
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 19-225 2.24e-58

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: 189.18  E-value: 2.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG---KDITALPPGKRNFGMVFQSyalfP-----N 90
Cdd:TIGR04520  17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENLWEIRKKVGMVFQN----PdnqfvG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:TIGR04520  93 ATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 171 EKLRREMRDLQEKVGVTTIMVTHDQEEALtMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:TIGR04520 173 KEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 7-222 2.71e-58

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: 187.19  E-value: 2.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQSY 85
Cdd:cd03265     3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 ALFPNLTALENIEygLKAKKYG--KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03265    83 SVDDELTGWENLY--IHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:cd03265   161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 5-224 3.32e-58

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: 187.89  E-value: 3.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNF 78
Cdd:TIGR02315   2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYG-LKAKK--------YGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGrLGYKPtwrsllgrFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 5-208 2.34e-57

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 184.61  E-value: 2.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAG-LEEA--TTGSIAVNGKDITALPPGKRNFGMV 81
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLkAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:COG4136    82 FQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVM 208
Cdd:COG4136   161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 7-275 6.22e-57

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 187.70  E-value: 6.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDA----FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-----KRN 77
Cdd:PRK11153    4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkaRRQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILL 157
Cdd:PRK11153   84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 158 LDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGS 237
Cdd:PRK11153  164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1003869982 238 InffsknneEHAIRPEH----VTVVQNNGMKTIVEsMEFRGS 275
Cdd:PRK11153  244 T--------LHLDLPEDylarLQAEPTTGSGPLLR-LEFTGE 276
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 5-229 3.14e-56

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 185.32  E-value: 3.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD-----------AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP 73
Cdd:COG4608     8 LEVRDLKKHFPvrgglfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 GK-----RNFGMVFQ-SYA-LFPNLTALENIEYGLKA-KKYGKAEVKEKALSALELVDLL-NVKDKYPAQMSGGQQQRVA 144
Cdd:COG4608    88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 145 LARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDqeeaLTM----ADKIVVMNHAEIMQIGTPE 220
Cdd:COG4608   168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRD 243


                  ....*....
gi 1003869982 221 EIYQRPANP 229
Cdd:COG4608   244 ELYARPLHP 252
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
 5-238 5.21e-56

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 182.72  E-value: 5.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNF------ 78
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNGPLvpadek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 ---------GMVFQSYALFPNLTALENI-EYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARA 148
Cdd:TIGR03005  81 hlrqmrnkiGMVFQSFNLFPHKTVLDNVtEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 149 LALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPAN 228
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240

                         250
                  ....*....|
gi 1003869982 229 PFVADFIGSI 238
Cdd:TIGR03005 241 ERTREFLSKV 250
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 1-218 5.57e-56

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 182.14  E-value: 5.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSeyLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTG--SIAVNGKDITALPPGK--- 75
Cdd:PRK11124    1 MS--IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSDKair 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 ---RNFGMVFQSYALFPNLTALEN-IEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALAL 151
Cdd:PRK11124   79 elrRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 152 SPDILLLDEPLSALDAKVREKLRREMRDLQEkVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGT 218
Cdd:PRK11124  159 EPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 5-235 1.12e-55

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 181.34  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAT-----TGSIAVNGKDITA----LPPGK 75
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGQDIYDkkidVVELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNFGMVFQSYALFPnLTALENIEYGLKAKKY-GKAEVKEKALSALELVDLLN-VKDK---YPAQMSGGQQQRVALARALA 150
Cdd:TIGR00972  82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDeVKDRlhdSALGLSGGQQQRLCIARALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238


                  ....*
gi 1003869982 231 VADFI 235
Cdd:TIGR00972 239 TEDYI 243
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 22-232 2.24e-55

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 184.16  E-value: 2.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG-------KDITaLPPGKRNFGMVFQSYALFPNLTAL 94
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIF-LPPEKRRIGYVFQEARLFPHLSVR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLKakkygKAEVKEKALSALELVDLLNVK---DKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVRE 171
Cdd:TIGR02142  94 GNLRYGMK-----RARPSERRISFERVIELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 172 KLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVA 232
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-235 3.71e-55

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 179.82  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSeyLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG-----------KDIT 69
Cdd:COG4161     1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  70 ALppgKRNFGMVFQSYALFPNLTALEN-IEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARA 148
Cdd:COG4161    79 LL---RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 149 LALSPDILLLDEPLSALDAKVREKLRREMRDLQEkVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTpEEIYQRPAN 228
Cdd:COG4161   156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233


                  ....*..
gi 1003869982 229 PFVADFI 235
Cdd:COG4161   234 EAFAHYL 240
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 14-235 2.52e-54

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 178.31  E-value: 2.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE-----ATTGSIAVNGKDI-------TALppgKRNFGMV 81
Cdd:COG1117    21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydpdvdvVEL---RRRVGMV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPnLTALENIEYGLK-AKKYGKAEVKEKALSALELVDLLN-VKDK---YPAQMSGGQQQRVALARALALSPDIL 156
Cdd:COG1117    98 FQKPNPFP-KSIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALWDeVKDRlkkSALGLSGGQQQRLCIARALAVEPEVL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 157 LLDEPLSALD----AKVrEKLrreMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVA 232
Cdd:COG1117   177 LMDEPTSALDpistAKI-EEL---ILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250


                  ...
gi 1003869982 233 DFI 235
Cdd:COG1117   251 DYI 253
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 5-222 2.64e-54

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: 176.93  E-value: 2.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF--DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMV 81
Cdd:cd03263     1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 162 LSALDAkvreKLRREMRDL--QEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:cd03263   161 TSGLDP----ASRRAIWDLilEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
5-208 3.99e-54

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 177.97  E-value: 3.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlPPGKRnfGMVFQS 84
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL 202
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 5-198 5.99e-54

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: 175.74  E-value: 5.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQ 83
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAkkYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG4133    83 ADGLKPELTVRENLRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEA 198
Cdd:COG4133   161 ALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-209 8.48e-54

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: 173.58  E-value: 8.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP--GKRNFGMVFQ 83
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 syalfpnltalenieyglkakkygkaevkekalsalelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd00267    81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMN 209
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
5-239 1.55e-53

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 180.61  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG------KRNF 78
Cdd:PRK10070   29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:PRK10070  109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSI 238
Cdd:PRK10070  189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268


                  .
gi 1003869982 239 N 239
Cdd:PRK10070  269 D 269
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 19-225 3.92e-53

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: 185.42  E-value: 3.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFpNLTALEN 96
Cdd:COG2274   490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeyglkakKYGKAEV-KEKALSALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:COG2274   569 I-------TLGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 165 LDAKVREKLRREMRDLqeKVGVTTIMVTHDqEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG2274   642 LDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 14-210 8.13e-52

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: 170.41  E-value: 8.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlppGKRNFGMVFQSYAL---FPn 90
Cdd:cd03235     9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSIdrdFP- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYG----KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:cd03235    85 ISVRDVVLMGLYGHKGLfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 167 AKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNH 210
Cdd:cd03235   165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNR 207
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 6-217 9.91e-52

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 169.15  E-value: 9.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQ 83
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 syalfpnltalenieyglkakkygkaevkekalsALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03214    81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03214   127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 5-222 1.22e-51

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: 170.31  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNF---GMV 81
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagiGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKygKAEVKEKALSALELVDLLNVKDKYPA-QMSGGQQQRVALARALALSPDILLLDE 160
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFPRLKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 7-210 1.23e-51

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 170.12  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDA-FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT-----ALPPGKRNFGM 80
Cdd:TIGR02673   4 FHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRIGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR02673  84 VFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLrreMRDLQE--KVGVTTIMVTHDQEEALTMADKIVVMNH 210
Cdd:TIGR02673 164 PTGNLDPDLSERI---LDLLKRlnKRGTTVIVATHDLSLVDRVAHRVIILDD 212
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
5-208 2.28e-51

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 169.51  E-value: 2.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFT----ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-----K 75
Cdd:NF038007    2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkiilR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNF-GMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:NF038007   82 RELiGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHdQEEALTMADKIVVM 208
Cdd:NF038007  162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINM 213
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-225 3.74e-51

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 170.97  E-value: 3.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFD--AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK--------DIta 70
Cdd:PRK13635    2 KEEIIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  71 lppgKRNFGMVFQSY-ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:PRK13635   80 ----RRQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK13635  156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-163 4.12e-51

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: 166.28  E-value: 4.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNLTALENI 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKAKKYGKAEVKEKALSALELVDLLNVKD----KYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 5-213 1.59e-50

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 168.70  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGkdiTALPPGKRNFGMVFQS 84
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKkygkaeVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK11247   90 ARLLPWKKVIDNVGLGLKGQ------WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 165 LDAKVreklRREMRDLQEKV----GVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK11247  164 LDALT----RIEMQDLIESLwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 18-213 1.86e-50

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 166.81  E-value: 1.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT-----ALPPGKRNFGMVFQSYALFPNLT 92
Cdd:cd03292    15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGVVFQDFRLLPDRN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAkvrEK 172
Cdd:cd03292    95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP---DT 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1003869982 173 LRREMRDLQE--KVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03292   172 TWEIMNLLKKinKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 24-217 3.31e-50

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 166.19  E-value: 3.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  24 SFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYALFPNLTALENIEYGLKA 103
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 104 KKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEK 183
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1003869982 184 VGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-224 4.83e-50

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 168.30  E-value: 4.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT----ALPPGKRNFGMVFQ--SYALFPNlT 92
Cdd:PRK13637   22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEE-T 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELV--DLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:PRK13637  101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 171 EKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK13637  181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 19-210 4.96e-50

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: 164.48  E-value: 4.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFpNLTALEN 96
Cdd:cd03228    17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGTIREN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeyglkakkygkaevkekalsalelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRRE 176
Cdd:cd03228    96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1003869982 177 MRDLQEkvGVTTIMVTHDqEEALTMADKIVVMNH 210
Cdd:cd03228   139 LRALAK--GKTVIVIAHR-LSTIRDADRIIVLDD 169
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
19-225 5.84e-50

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 174.97  E-value: 5.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFpNLTALEN 96
Cdd:COG1132   355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIREN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGlkAKKYGKAEVKE--KALSALELVDLLnvKDKYPAQ-------MSGGQQQRVALARALALSPDILLLDEPLSALD- 166
Cdd:COG1132   434 IRYG--RPDATDEEVEEaaKAAQAHEFIEAL--PDGYDTVvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDt 509

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 167 ---AKVREKLRREMRdlqekvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEE------IYQR 225
Cdd:COG1132   510 eteALIQEALERLMK------GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEllarggLYAR 570
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 11-229 9.07e-50

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: 173.72  E-value: 9.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  11 QKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEaTTGSIAVNGKDITALP-----PGKRNFGMVFQS- 84
Cdd:COG4172   293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDp 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YA-LFPNLTALENIEYGLKAKKYG--KAEVKEKALSALELVDLL-NVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG4172   372 FGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDqeeaL----TMADKIVVMNHAEIMQIGTPEEIYQRPANP 229
Cdd:COG4172   452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LavvrALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 20-208 1.19e-49

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 165.19  E-value: 1.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-----TALPPGKRNFGMVFQSYALFPNLTAL 94
Cdd:TIGR02982  21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaskKQLVQLRRRIGYIFQAHNLLGFLTAR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLK-AKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:TIGR02982 101 QNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDV 180

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1003869982 174 RREMRDLQEKVGVTTIMVTHDQeEALTMADKIVVM 208
Cdd:TIGR02982 181 VELMQKLAKEQGCTILMVTHDN-RILDVADRILQM 214
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 7-206 2.11e-49

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 163.94  E-value: 2.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNF-GM 80
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREKlGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEAlTMADKIV 206
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRVI 204
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 19-222 3.79e-49

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 165.55  E-value: 3.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSY-ALFPNLTALE 95
Cdd:PRK13632   24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQNPdNQFIGATVED 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRR 175
Cdd:PRK13632  104 DIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1003869982 176 EMRDLQEKVGVTTIMVTHDQEEALtMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK13632  184 IMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 15-225 4.55e-49

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: 172.25  E-value: 4.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPnLT 92
Cdd:COG4988   348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQNPYLFA-GT 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIeyGLKAKKYGKAEVKEkalsALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:COG4988   427 IRENL--RLGRPDASDEELEA----ALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 162 LSALDAKVREKLRREMRDLQEkvGVTTIMVTHDqEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG4988   501 TAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 7-236 2.45e-48

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 162.61  E-value: 2.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-TALPPGKR--------- 76
Cdd:PRK11264    6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQkglirqlrq 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 NFGMVFQSYALFPNLTALEN-IEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:PRK11264   86 HVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 156 LLLDEPLSALDAKVREKLRREMRDL-QEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANP----F 230
Cdd:PRK11264  166 ILFDEPTSALDPELVGEVLNTIRQLaQEK--RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPrtrqF 243


                  ....*.
gi 1003869982 231 VADFIG 236
Cdd:PRK11264  244 LEKFLL 249
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 22-217 3.82e-48

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: 160.74  E-value: 3.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYALFPNLTALENIEYGL 101
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 102 KAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQ 181
Cdd:cd03298    96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1003869982 182 EKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03298   176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
8-207 4.75e-48

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 161.29  E-value: 4.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   8 QHIQKQFDaftalkdisFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQSYAL 87
Cdd:PRK10771   12 HHLPMRFD---------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNLTALENIEYG----LKAKKYGKAEVKEKAlsalELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK10771   83 FSHLTVAQNIGLGlnpgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1003869982 164 ALDAkvreKLRREMRDLQEKV----GVTTIMVTHDQEEALTMADKIVV 207
Cdd:PRK10771  159 ALDP----ALRQEMLTLVSQVcqerQLTLLMVSHSLEDAARIAPRSLV 202
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 18-227 7.38e-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: 166.48  E-value: 7.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFpNLTALE 95
Cdd:COG4987   349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTTLRE 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIeyglkakKYGKAEVKEKAL-SALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG4987   428 NL-------RLARPDATDEELwAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTE 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 164 ALDAKVREKLRREMRD-LQEKvgvTTIMVTHDqEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:COG4987   501 GLDAATEQALLADLLEaLAGR---TVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 5-209 9.67e-47

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: 156.99  E-value: 9.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS 84
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEkalsALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03268    81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1003869982 165 LDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMN 209
Cdd:cd03268   157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIIN 200
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 5-225 1.06e-46

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 159.89  E-value: 1.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPpgKRNFGmvfqs 84
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIG----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 Y-----ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:COG4152    75 YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 160 EPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG4152   155 EPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
cbiO PRK13650
energy-coupling factor transporter ATPase;
20-225 1.43e-46

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 159.13  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSY-ALFPNLTALEN 96
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRRE 176
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 177 MRDLQEKVGVTTIMVTHDQEEaLTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
5-208 4.47e-46

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 162.88  E-value: 4.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-RNFG--MV 81
Cdd:COG1129     5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGiaII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKYG---KAEVKEKALSALELVDL-LNVKDKYpAQMSGGQQQRVALARALALSPDILL 157
Cdd:COG1129    85 HQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLdIDPDTPV-GDLSVAQQQLVEIARALSRDARVLI 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 158 LDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:COG1129   164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-208 7.25e-46

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 162.50  E-value: 7.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG---KRN 77
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYGLKAKKYG---KAEVKEK--ALSA---LElVDLlnvkDKYPAQMSGGQQQRVALARAL 149
Cdd:COG3845    82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARirELSErygLD-VDP----DAKVEDLSVGEQQRVEILKAL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:COG3845   157 YRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVL 214
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 5-227 7.39e-46

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: 155.53  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN---FGMV 81
Cdd:COG0410     4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKyGKAEVKEkalsALELV-DLL-NVKDKY--PA-QMSGGQQQRVALARALALSPDIL 156
Cdd:COG0410    84 PEGRRIFPSLTVEENLLLGAYARR-DRAEVRA----DLERVyELFpRLKERRrqRAgTLSGGEQQMLAIGRALMSRPKLL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 157 LLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:COG0410   159 LLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 5-217 2.86e-45

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: 153.68  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDA----FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALP-PGKRNFG 79
Cdd:cd03266     2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENIEY-----GLKAKKYgKAEVKEKAlSALELVDLLnvkDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYfaglyGLKGDEL-TARLEELA-DRLGMEELL---DRRVGGFSTGMRQKVAIARALVHDPP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03266   157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-225 3.41e-45

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 154.08  E-value: 3.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQF----------------------DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT 58
Cdd:COG1134     1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  59 GSIAVNGKdITALppgkRNFGMVFQsyalfPNLTALENIE-----YGLKakkygKAEVKEK-----ALSALElvDLLN-- 126
Cdd:COG1134    81 GRVEVNGR-VSAL----LELGAGFH-----PELTGRENIYlngrlLGLS-----RKEIDEKfdeivEFAELG--DFIDqp 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 127 VKdKYpaqmSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIV 206
Cdd:COG1134   144 VK-TY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAI 217

                         250
                  ....*....|....*....
gi 1003869982 207 VMNHAEIMQIGTPEEIYQR 225
Cdd:COG1134   218 WLEKGRLVMDGDPEEVIAA 236
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 5-227 4.12e-45

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 153.85  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-NFGMVF- 82
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 -QSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:cd03218    81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 162 LSALDAKVREKLRREMRDLQEK-VGvttIMVT-HDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 20-209 7.67e-45

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 152.51  E-value: 7.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR------NFGMVFQSYALFPNLTA 93
Cdd:TIGR02211  21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFTA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1003869982 174 RREMRDLQEKVGVTTIMVTHDQEEALTMaDKIVVMN 209
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMK 215
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 5-217 1.06e-44

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: 151.96  E-value: 1.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVcLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN-FGMVFQ 83
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 164 ALDAKVREKLRREMRDLQEkvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03264   160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 6-213 1.42e-44

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: 151.26  E-value: 1.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDItalPPGKR--NFGMVF 82
Cdd:cd03226     1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERrkSIGYVM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QS--YALFPNlTALENIEYGLKAKkYGKAEVKEKALSALELVDLlnvKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:cd03226    78 QDvdYQLFTD-SVREELLLGLKEL-DAGNEQAETVLKDLDLYAL---KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 161 PLSALDAKVREKLRREMRDLQeKVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03226   153 PTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 5-217 1.67e-44

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: 151.28  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPpgKRNFGMVFQS 84
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 165 LDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03269   159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
5-226 1.73e-44

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 152.96  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG----KRnfGM 80
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRR--AV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYAL-FPnLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALA-------LS 152
Cdd:COG4559    80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDL-QEKVGVttIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:COG4559   159 PRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGV--VAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 5-231 2.29e-44

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 152.11  E-value: 2.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-NFGMvfq 83
Cdd:COG1137     4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRaRLGI--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SY-----ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:COG1137    81 GYlpqeaSIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEK-VGVttiMVT-HDQEEALTMADKIVVMNHAEIMQIGTPEEIYqrpANPFV 231
Cdd:COG1137   161 DEPFAGVDPIAVADIQKIIRHLKERgIGV---LITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL---NNPLV 229
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-229 6.32e-44

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 151.53  E-value: 6.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFD---------AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKditAL 71
Cdd:COG4167     1 MSALLEVRNLSKTFKyrtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  72 PPGK-----RNFGMVFQ--SYALFPNLTALENIEYGLK-AKKYGKAEVKEKALSALELVDLL-NVKDKYPAQMSGGQQQR 142
Cdd:COG4167    78 EYGDykyrcKHIRMIFQdpNTSLNPRLNIGQILEEPLRlNTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 143 VALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG4167   158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237


                  ....*..
gi 1003869982 223 YQRPANP 229
Cdd:COG4167   238 FANPQHE 244
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 5-213 6.55e-44

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: 148.35  E-value: 6.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-RNFG--MV 81
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGiaMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQsyalfpnltalenieyglkakkygkaevkekalsalelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:cd03216    81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03216   110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-235 9.39e-44

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 150.89  E-value: 9.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSE-YLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT---------- 69
Cdd:PRK10619    1 MSEnKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  70 -----ALPPGKRNFGMVFQSYALFPNLTALENI-EYGLKAKKYGKAEVKEKALSALELVDLLN-VKDKYPAQMSGGQQQR 142
Cdd:PRK10619   81 vadknQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 143 VALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239

                         250
                  ....*....|...
gi 1003869982 223 YQRPANPFVADFI 235
Cdd:PRK10619  240 FGNPQSPRLQQFL 252
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 19-227 1.96e-43

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 150.94  E-value: 1.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA------LPPGKRNFGMVFQ--SYALFPN 90
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLRKKVGIVFQfpEHQLFEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 lTALENIEYGLKAKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:PRK13634  102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 170 REKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:PRK13634  181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 5-221 4.10e-43

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 149.15  E-value: 4.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVF 82
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYAL-FPnLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALA-LS-----PDI 155
Cdd:PRK13548   83 QHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqLWepdgpPRW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 156 LLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEE 221
Cdd:PRK13548  162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 5-229 5.22e-43

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 155.23  E-value: 5.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDA----FTALKDISFTVKKNEFVCLLGPSGCGKT----TLLRILAGLEEATTGSIAVNGKDITALPP--- 73
Cdd:COG4172     7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSErel 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 ----GKRnFGMVFQ--SYALFPNLTALENIEYGLKA-KKYGKAEVKEKALSALELVDLLNVK---DKYPAQMSGGQQQRV 143
Cdd:COG4172    87 rrirGNR-IAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 144 ALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDqeeaLT----MADKIVVMNHAEIMQIGTP 219
Cdd:COG4172   166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPT 241

                         250
                  ....*....|
gi 1003869982 220 EEIYQRPANP 229
Cdd:COG4172   242 AELFAAPQHP 251
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 11-224 1.44e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 145.66  E-value: 1.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  11 QKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQS-YAL 87
Cdd:PRK13648   16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQNpDNQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:PRK13648   96 FVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 168 KVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK13648  176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 5-213 2.21e-41

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 144.84  E-value: 2.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFT-----ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR--N 77
Cdd:COG1101     2 LELKNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYAL--FPNLTALEN--IEYgLKAKKYG---------KAEVKEKaLSALE--LVDLLNVKDKYpaqMSGGQQQR 142
Cdd:COG1101    82 IGRVFQDPMMgtAPSMTIEENlaLAY-RRGKRRGlrrgltkkrRELFREL-LATLGlgLENRLDTKVGL---LSGGQRQA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 143 VALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:COG1101   157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
5-215 2.47e-41

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 144.83  E-value: 2.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF---------DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALP-PG 74
Cdd:PRK10419    4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNrAQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 KRNF----GMVFQSY--ALFPNLTALENIEYGLK-AKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALA 146
Cdd:PRK10419   84 RKAFrrdiQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 147 RALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQ 215
Cdd:PRK10419  164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 18-215 2.75e-41

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: 144.95  E-value: 2.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-----KRNFGMVFQ-SYALF-PN 90
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQdSPSAVnPR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLK-AKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1003869982 169 VREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQ 215
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 19-230 2.86e-41

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 146.26  E-value: 2.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-----KRNFGMVFQS-YA-LFPNL 91
Cdd:PRK11308   30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNPRK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAK-KYGKAEVKEKALSALELVDLlnvK----DKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK11308  110 KVGQILEEPLLINtSLSAAERREKALAMMAKVGL---RpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 167 AKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK11308  187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 5-222 1.61e-40

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: 141.51  E-value: 1.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR---NFGMV 81
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALsALELVdLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIY-ELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 5-222 1.97e-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: 142.15  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTG-SIAVNGK-----DITALppgKRNF 78
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDVWEL---RKRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVfqSYALF----PNLTALENIEYGLKA-----KKYGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:COG1119    81 GLV--SPALQlrfpRDETVLDVVLSGFFDsiglyREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG1119   158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 15-225 2.69e-40

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: 141.21  E-value: 2.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFpNLT 92
Cdd:cd03253    12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTVLF-NDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYG-LKAkkyGKAEVKEKALSALELVDLLNVKDKYPAQ-------MSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03253    91 IGYNIRYGrPDA---TDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 165 LDAKVREKLRREMRDLQEkvGVTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:cd03253   168 LDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-235 2.89e-40

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 141.84  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL-----EEATTGSIAVNGKDI----TAL 71
Cdd:PRK14239    2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  72 PPGKRNFGMVFQSYALFPnLTALENIEYGLKAK----KYGKAEVKEKALSALELVDllNVKDKYPAQ---MSGGQQQRVA 144
Cdd:PRK14239   82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIWD--EVKDRLHDSalgLSGGQQQRVC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 145 LARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK14239  159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236

                         250
                  ....*....|.
gi 1003869982 225 RPANPFVADFI 235
Cdd:PRK14239  237 NPKHKETEDYI 247
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 20-225 4.92e-40

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: 140.75  E-value: 4.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALENI 97
Cdd:cd03249    19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLFDG-TIAENI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGlkaKKYGKAEVKEKALSALELVDLL-NVKDKYP-------AQMSGGQQQRVALARALALSPDILLLDEPLSALDAK- 168
Cdd:cd03249    98 RYG---KPDATDEEVEEAAKKANIHDFImSLPDGYDtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEs 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 169 ---VREKLRREMRdlqekvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:cd03249   175 eklVQEALDRAMK------GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 5-198 8.99e-40

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 139.91  E-value: 8.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF----DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR---- 76
Cdd:PRK10584    7 VEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 --NFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPD 154
Cdd:PRK10584   87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEA 198
Cdd:PRK10584  167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 19-213 1.95e-39

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: 137.18  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-NFGMVF-----QSYALFPNLT 92
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIeyglkakkygkaevkekALSALelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:cd03215    95 VAENI-----------------ALSSL---------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1003869982 173 LRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03215   143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 19-230 2.15e-39

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 141.77  E-value: 2.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-----NFGMVFQS--YALFPNL 91
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKA--KKYGKAEVKEKALSALELVDLL-NVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:PRK15079  116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 169 VREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK15079  196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
cbiO PRK13641
energy-coupling factor transporter ATPase;
20-226 2.76e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 140.35  E-value: 2.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA------LPPGKRNFGMVFQ--SYALFPNl 91
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknLKKLRKKVSLVFQfpEAQLFEN- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:PRK13641  102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 171 EKLRREMRDLQeKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK13641  182 KEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
22-238 4.72e-39

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 139.13  E-value: 4.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNFGMVFQSYALFPNLTALEN 96
Cdd:PRK11831   25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFTDMNVFDN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKAKKYGKAEV-KEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRR 175
Cdd:PRK11831  105 VAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 176 EMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPaNPFVADFIGSI 238
Cdd:PRK11831  185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 1-226 8.42e-39

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 137.81  E-value: 8.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEY-LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-RNF 78
Cdd:PRK11300    1 MSQPlLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMV--FQSYALFPNLTALEN------------IEYGL-KAKKYGKAEVK--EKALSALELVDLLNVKDKYPAQMSGGQQQ 141
Cdd:PRK11300   81 GVVrtFQHVRLFREMTVIENllvaqhqqlktgLFSGLlKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 142 RVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEE 221
Cdd:PRK11300  161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240


                  ....*
gi 1003869982 222 IYQRP 226
Cdd:PRK11300  241 IRNNP 245
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 17-217 1.17e-38

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: 136.51  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKdITALPpgkrNFGMVFQsyalfPNLTALEN 96
Cdd:cd03220    35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLL----GLGGGFN-----PELTGREN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IE-----YGLKAKkygkaEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVRE 171
Cdd:cd03220   105 IYlngrlLGLSRK-----EIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 172 KLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03220   180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
cbiO PRK13640
energy-coupling factor transporter ATPase;
19-226 1.46e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 138.01  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL---EEATTGSIAVNGKDITA--LPPGKRNFGMVFQSY-ALFPNLT 92
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVGAT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:PRK13640  102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 173 LRREMRDLQEKVGVTTIMVTHDQEEAlTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK13640  182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-211 1.83e-38

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: 136.41  E-value: 1.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFD-------AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK----DIT 69
Cdd:COG4778     1 MTTLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  70 ALPPG------KRNFGMVFQsyalF----PNLTALENIEYGLKAKKYGKAEVKEKALsalELVDLLNVKDK----YPAQM 135
Cdd:COG4778    81 QASPReilalrRRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARAR---ELLARLNLPERlwdlPPATF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 136 SGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHA 211
Cdd:COG4778   154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 15-239 2.09e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 137.52  E-value: 2.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI----TALPPGKRNFGMVFQSY--ALF 88
Cdd:PRK13639   13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVGIVFQNPddQLF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  89 PNlTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:PRK13639   93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 169 VREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ-----RPAN---PFVADFIGSIN 239
Cdd:PRK13639  172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdietiRKANlrlPRVAHLIEILN 249
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 19-224 4.10e-38

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 143.47  E-value: 4.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALEN 96
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGlkAKKYGKAEVkekaLSALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:TIGR03375 559 IALG--APYADDEEI----LRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 166 DAKVREKLRREMRDLQEkvGVTTIMVTHDQeEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:TIGR03375 633 DNRSEERFKDRLKRWLA--GKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLE 688
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 19-213 4.60e-38

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: 135.02  E-value: 4.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALEN 96
Cdd:cd03245    19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKAKKygkaevKEKALSALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:cd03245    98 ITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 166 D----AKVREKLRREMRDlqekvgVTTIMVTHDQeEALTMADKIVVMNHAEI 213
Cdd:cd03245   172 DmnseERLKERLRQLLGD------KTLIIITHRP-SLLDLVDRIIVMDSGRI 216
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 19-208 6.52e-38

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: 141.66  E-value: 6.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALEN 96
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-TIAEN 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeygLKAKKYGKAEVKEKALSALELVDLLNVK--------DKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:TIGR02857 416 I---RLARPDASDAEIREALERAGLDEFVAALpqgldtpiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1003869982 169 VREKLRREMRDLQEkvGVTTIMVTHDqEEALTMADKIVVM 208
Cdd:TIGR02857 493 TEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 15-225 9.05e-38

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: 134.67  E-value: 9.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFpNLT 92
Cdd:cd03251    13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGlkAKKYGKAEVKE--KALSALELVDllNVKDKYPA-------QMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:cd03251    92 VAENIAYG--RPGATREEVEEaaRAANAHEFIM--ELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPILILDEATS 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 164 ALDAKVREKLRREMRDLQEkvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:cd03251   168 ALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 22-228 1.15e-37

nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 134.42  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTT----LLRILAGLEEATTGSIAVNGKDITALPPGKRNFGMVFQS--YALFPNLTALE 95
Cdd:TIGR02770   4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIEYGLKAKKYGKAEVKEKALSALELVDLLNVK---DKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:TIGR02770  84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 173 LRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPAN 228
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 5-222 1.36e-37

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: 134.32  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR---NFGMV 81
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLK-AKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR04406  82 PQEASIFRKLTVEENIMAVLEiRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 5-210 2.63e-37

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: 132.59  E-value: 2.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKditalppgkrnFGMVFQS 84
Cdd:cd03250     6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 yALFPNLTALENIEYGLK--AKKYGKAeVK----EKALSALELVDLLNVKDKyPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:cd03250    75 -PWIQNGTIRENILFGKPfdEERYEKV-IKacalEPDLEILPDGDLTEIGEK-GINLSGGQKQRISLARAVYSDADIYLL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 159 DEPLSALDAKVREKL-----RREMRDlqekvGVTTIMVTHdQEEALTMADKIVVMNH 210
Cdd:cd03250   152 DDPLSAVDAHVGRHIfenciLGLLLN-----NKTRILVTH-QLQLLPHADQIVVLDN 202
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 20-209 2.97e-37

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: 131.18  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALENI 97
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYLPQDDELFSG-SIAENI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 eyglkakkygkaevkekalsalelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREM 177
Cdd:cd03246    97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1003869982 178 RDLQeKVGVTTIMVTHdQEEALTMADKIVVMN 209
Cdd:cd03246   140 AALK-AAGATRIVIAH-RPETLASADRILVLE 169
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
35-227 4.49e-37

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 135.77  E-value: 4.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  35 LLGPSGCGKTTLLRILAGLEEATTGSIAVNGK---DI---TALPPGKRNFGMVFQSYALFPNLTALENIEYGLKAKKygK 108
Cdd:PRK11144   29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSM--V 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 109 AEVkekalsaLELVDLLNVK---DKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVG 185
Cdd:PRK11144  107 AQF-------DKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1003869982 186 VTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:PRK11144  180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
cbiO PRK13646
energy-coupling factor transporter ATPase;
17-223 6.70e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 133.75  E-value: 6.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA------LPPGKRNFGMVFQsyalFPN 90
Cdd:PRK13646   20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALEN-----IEYGLKAKKYGKAEVKEKALSAL-ELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK13646   96 SQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK13646  176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 5-226 8.39e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 132.73  E-value: 8.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL-----EEATTGSIAVNGKDITALPPG--KRN 77
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIelRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYGLKAKKY--GKAEVKEKALSALELVDLLN-VKDKYPA---QMSGGQQQRVALARALAL 151
Cdd:PRK14247   84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDeVKDRLDApagKLSGGQQQRLCIARALAF 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 152 SPDILLLDEPLSALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK14247  164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 19-225 3.54e-36

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: 130.42  E-value: 3.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALEN 96
Cdd:cd03254    18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTFLFSG-TIMEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGlkaKKYGKAEVKEKALSALELVDLL-NVKDKYPAQM-------SGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:cd03254    97 IRLG---RPNATDEEVIEAAKEAGAHDFImKLPNGYDTVLgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 169 VREKLRREMRDLQEkvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:cd03254   174 TEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-239 3.60e-36

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 137.93  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQF----DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-- 74
Cdd:PRK10535    1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADal 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 ----KRNFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALA 150
Cdd:PRK10535   81 aqlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEAlTMADKIVVMNHAEIM--------QIGTPEEI 222
Cdd:PRK10535  161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVrnppaqekVNVAGGTE 238

                         250
                  ....*....|....*..
gi 1003869982 223 YQRPANPFVADFIGSIN 239
Cdd:PRK10535  239 PVVNTASGWRQFVSGFR 255
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 6-214 9.38e-36

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: 129.37  E-value: 9.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQK-QFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGkditaLPPGKR------NF 78
Cdd:cd03267    22 SLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRrkkflrRI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 GMVF-QSYALFPNLTALENIE-----YGLKAKKYgKAEVKEkalsaleLVDLLNVKD--KYPA-QMSGGQQQRVALARAL 149
Cdd:cd03267    97 GVVFgQKTQLWWDLPVIDSFYllaaiYDLPPARF-KKRLDE-------LSELLDLEEllDTPVrQLSLGQRMRAEIAAAL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 150 ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIM 214
Cdd:cd03267   169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 17-235 1.06e-35

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 130.29  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE-----ATTGSIAVNGKDITA--LPPG--KRNFGMVFQSYAL 87
Cdd:PRK14243   23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYApdVDPVevRRRIGMVFQKPNP 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNlTALENIEYGLKAKKY--GKAEVKEKALSALELVDllNVKDKYPAQ---MSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:PRK14243  103 FPK-SIYDNIAYGARINGYkgDMDELVERSLRQAALWD--EVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 163 SALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMN---------HAEIMQIGTPEEIYQRPANPFVAD 233
Cdd:PRK14243  180 SALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQATRD 257


                  ..
gi 1003869982 234 FI 235
Cdd:PRK14243  258 YV 259
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 19-226 1.60e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 129.92  E-value: 1.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSY--ALFpNLTAL 94
Cdd:PRK13652   19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNPddQIF-SPTVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLR 174
Cdd:PRK13652   98 QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 175 REMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK13652  178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 20-225 1.97e-35

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 134.88  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFPNlTALENI 97
Cdd:COG4618   348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 eyglkAKkYGKAEVkEKALSALELVDL----LNVKDKY-------PAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:COG4618   427 -----AR-FGDADP-EKVVAAAKLAGVhemiLRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 167 AKVREKLRREMRDLQEKvGVTTIMVTHDQeEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG4618   500 DEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-223 2.45e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 129.44  E-value: 2.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHI----QKQFDAfTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPG 74
Cdd:PRK13642    1 MNKILEVENLvfkyEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 KRNFGMVFQSY-ALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSP 153
Cdd:PRK13642   80 RRKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 154 DILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK13642  160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
5-224 3.33e-35

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 128.59  E-value: 3.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPgkRNFGmvfQS 84
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS--RQLA---RR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPN-------LTALENIEYGLKA--KKYGKAEVKEKAL--SALELVDLLNVKDKYPAQMSGGQQQRVALARALALSP 153
Cdd:PRK11231   78 LALLPQhhltpegITVRELVAYGRSPwlSLWGRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 154 DILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK11231  158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 3-227 4.17e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 129.97  E-value: 4.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   3 EYLSIQHI-----QKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAV----NGKDITALPP 73
Cdd:PRK13631   20 IILRVKNLycvfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 G--------------KRNFGMVFQ--SYALFPNlTALENIEYGLKAKKYGKAEVKEKALSALELVDL-LNVKDKYPAQMS 136
Cdd:PRK13631  100 ItnpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 137 GGQQQRVALARALALSPDILLLDEPLSALDAKVreklRREMRDL---QEKVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK13631  179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG----EHEMMQLildAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254

                         250
                  ....*....|....
gi 1003869982 214 MQIGTPEEIYQRPA 227
Cdd:PRK13631  255 LKTGTPYEIFTDQH 268
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
18-223 7.18e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 128.28  E-value: 7.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG---KDITALPPGKRNFGMVFQSyalfPN--LT 92
Cdd:PRK13633   24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqIV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 AL---ENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:PRK13633  100 ATiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 170 REKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK13633  180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 20-235 7.50e-35

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 127.65  E-value: 7.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL----EEA-TTGSIAVNGKDITALPPG----KRNFGMVFQSYALFPN 90
Cdd:PRK14267   20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelnEEArVEGEVRLFGRNIYSPDVDpievRREVGMVFQYPNPFPH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKY--GKAEVKEKALSALELVDLLN-VKDK---YPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK14267  100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDeVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 165 LD----AKVREKLrremrdLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFI 235
Cdd:PRK14267  180 IDpvgtAKIEELL------FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 2-215 1.87e-34

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 125.60  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   2 SEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFG 79
Cdd:PRK10247    5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNlTALENIEYGLKAKKygKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:PRK10247   85 YCAQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEaLTMADKIVVMN-HAEIMQ 215
Cdd:PRK10247  162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQpHAGEMQ 218
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 6-226 1.90e-34

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 126.35  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   6 SIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQ 83
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYG--------LKAKKYgkaEVKEKALSALELVDLlnvKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:COG4604    83 ENHINSRLTVRELVAFGrfpyskgrLTAEDR---EIIDEAIAYLDLEDL---ADRYLDELSGGQRQRAFIAMVLAQDTDY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 156 LLLDEPLSALDAK-VREKLRReMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:COG4604   157 VLLDEPLNNLDMKhSVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
19-194 2.27e-34

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 125.37  E-value: 2.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAL-----PPGKRNFGMVFQSYALFPNLTA 93
Cdd:PRK10908   17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQIGMIFQDHHLLMDRTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:PRK10908   97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176

                         170       180
                  ....*....|....*....|.
gi 1003869982 174 RREMRDLQeKVGVTTIMVTHD 194
Cdd:PRK10908  177 LRLFEEFN-RVGVTVLMATHD 196
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 15-220 2.93e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 126.39  E-value: 2.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSY--ALFPN 90
Cdd:PRK13647   16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVFSS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 lTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:PRK13647   96 -TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003869982 171 EKLrREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPE 220
Cdd:PRK13647  175 ETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
20-194 1.63e-33

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 123.39  E-value: 1.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG------KRNFGMVFQSYALFPNLTA 93
Cdd:PRK11629   25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:PRK11629  105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184

                         170       180
                  ....*....|....*....|.
gi 1003869982 174 RREMRDLQEKVGVTTIMVTHD 194
Cdd:PRK11629  185 FQLLGELNRLQGTAFLVVTHD 205
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 18-230 4.20e-33

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 128.28  E-value: 4.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTT----LLRILAgleeaTTGSIAVNGKDI-----TALPPGKRNFGMVFQ--SYA 86
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhnlnrRQLLPVRHRIQVVFQdpNSS 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENIEYGLKA--KKYGKAEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK15134  375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK15134  455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 7-194 4.52e-33

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 127.87  E-value: 4.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVngkditalPPGKRnFGMVFQSYA 86
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENIEYGLK----------------------AKKYGKAEVK-------------EKALSALEL--VDLlnvkD 129
Cdd:COG0488    72 LDDDLTVLDTVLDGDAelraleaeleeleaklaepdedLERLAELQEEfealggweaearaEEILSGLGFpeEDL----D 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 130 KYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQekvgVTTIMVTHD 194
Cdd:COG0488   148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
cbiO PRK13645
energy-coupling factor transporter ATPase;
17-223 5.78e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 123.58  E-value: 5.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTG-------SIAVNGKDITALPPGKRNFGMVFQ--SYAL 87
Cdd:PRK13645   24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRKEIGLVFQfpEYQL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNlTALENIEYGLKAKKYGKAEVKEKALsalELVDLLNVKDKY----PAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK13645  104 FQE-TIEKDIAFGPVNLGENKQEAYKKVP---ELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 164 ALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK13645  180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 20-235 6.24e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 122.46  E-value: 6.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK------DITALPPGK--RNFGMVFQSYALFPNL 91
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKlrKEVGMVFQQPNPFPHL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAKKYG-KAEVKEKALSALELVDLLN-VKDKY--PA-QMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK14246  106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKeVYDRLnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 167 AKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFI 235
Cdd:PRK14246  186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 20-208 1.01e-32

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: 119.96  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL--EEATTGSIAVNGKDITALPPGKRnFGMVFQSYALFPNLTALENI 97
Cdd:cd03213    25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKAKkygkaevkekalsalelvdllnvkdkypaQMSGGQQQRVALARALALSPDILLLDEPLSALDA----KVREKL 173
Cdd:cd03213   104 MFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSssalQVMSLL 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1003869982 174 RREMRDlqekvGVTTIMVTHD-QEEALTMADKIVVM 208
Cdd:cd03213   155 RRLADT-----GRTIICSIHQpSSEIFELFDKLLLL 185
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 18-225 1.61e-32

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 122.89  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG----KDITALppgKRNFGMVF-QSYALFPNLT 92
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEF---ARRIGVVFgQRSQLWWDLP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIE-----YGLKAKKYgkaevkEKALSalELVDLLNVKDKY--PA-QMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:COG4586   113 AIDSFRllkaiYRIPDAEY------KKRLD--ELVELLDLGELLdtPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQE--EALtmADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:COG4586   185 LDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGSLEELKER 245
cbiO PRK13649
energy-coupling factor transporter ATPase;
19-225 2.32e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 121.78  E-value: 2.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA------LPPGKRNFGMVFQsyalFPNL- 91
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 ----TALENIEYGLKAKKYGKAEVKEKALSALELVDLL-NVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK13649   98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 167 AKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK13649  178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-221 4.15e-32

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 120.50  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL--EEATTGS--------IAVNGKDITA 70
Cdd:PRK09984    1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  71 LPPGKRNFGMVFQSYALFPNLTALENIEYGLKAK--------KYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQR 142
Cdd:PRK09984   81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 143 VALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEE 221
Cdd:PRK09984  161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
19-222 4.83e-32

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 124.75  E-value: 4.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNfGMVF-----QSYALFPNL 91
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRA-GIAYvpedrKGEGLVLDL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLkAKKYGKA----EVKEKALsALELVDLLNVKDKYPAQ----MSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG1129   346 SIRENITLAS-LDRLSRGglldRRRERAL-AEEYIKRLRIKTPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTR 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG1129   424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 19-222 6.00e-32

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: 124.91  E-value: 6.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAV----NGKDITALPP-----GKRNFGMVFQSYALFP 89
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPdgrgrAKRYIGILHQEYDLYP 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  90 NLTALENIEYGLkAKKYGKAEVKEKALSALELVDL-----LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:TIGR03269 379 HRTVLDNLTEAI-GLELPDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 165 LDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
cbiO PRK13644
energy-coupling factor transporter ATPase;
15-227 7.67e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 120.09  E-value: 7.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG---KDITALPPGKRNFGMVFQS-YALFPN 90
Cdd:PRK13644   13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:PRK13644   93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 171 EKLRREMRDLQEKvGVTTIMVTHDQEEaLTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:PRK13644  173 IAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 19-230 1.03e-31

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 124.97  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-----RNFGMVFQS-YA-LFPNL 91
Cdd:PRK10261  339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAKKYGKAEVKEKALS-ALELVDLLNVKD-KYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:PRK10261  419 TVGDSIMEPLRVHGLLPGKAAAARVAwLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 170 REKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK10261  499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
5-222 1.23e-31

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 120.30  E-value: 1.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-TALPPGKRNFGMVFQ 83
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIE-----YGLKAkkygkAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:PRK13537   88 FDNLDPDFTVRENLLvfgryFGLSA-----AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK13537  163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
cbiO PRK13643
energy-coupling factor transporter ATPase;
16-224 1.93e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 119.45  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  16 AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA------LPPGKRNFGMVFQ--SYAL 87
Cdd:PRK13643   18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGVVFQfpESQL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNlTALENIEYGLKAKKYGKAEVKEKALSALELVDLLN-VKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK13643   98 FEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 167 AKVREKLRREMRDLQEkVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK13643  177 PKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 5-238 2.21e-31

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 118.39  E-value: 2.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKD-----ITALPPGKRNF- 78
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  79 -----GMVFQSYA--LFPNLTALENIEYGLKA---KKYGKaeVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRVALAR 147
Cdd:TIGR02323  84 mrtewGFVHQNPRdgLRMRVSAGANIGERLMAigaRHYGN--IRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 148 ALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPA 227
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241

                         250
                  ....*....|.
gi 1003869982 228 NPFVADFIGSI 238
Cdd:TIGR02323 242 HPYTQLLVSSI 252
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 10-222 2.53e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 119.42  E-value: 2.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDA-----FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKD----------------I 68
Cdd:PRK13651    8 IVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlekL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  69 TALPPGKRNF----------GMVFQ--SYALFPNlTALENIEYGLKAKKYGKAEVKEKALSALELVDL-LNVKDKYPAQM 135
Cdd:PRK13651   88 VIQKTRFKKIkkikeirrrvGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 136 SGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQ 215
Cdd:PRK13651  167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245


                  ....*..
gi 1003869982 216 IGTPEEI 222
Cdd:PRK13651  246 DGDTYDI 252
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 20-222 3.19e-31

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: 123.23  E-value: 3.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFPNlTALENI 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 eyglkaKKYGKAEVKEKALSALELVD----LLNVKDKYP-------AQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:TIGR01842 413 ------ARFGENADPEKIIEAAKLAGvhelILRLPDGYDtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 167 AKVREKLRREMRDLQEKvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:TIGR01842 487 EEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 15-225 4.62e-31

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: 117.20  E-value: 4.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLT 92
Cdd:cd03252    13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELVDLL-----NVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:cd03252    92 IRDNIALADPGMSMERVIEAAKLAGAHDFISELpegydTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 168 KVREKLRREMRDLQEkvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:cd03252   172 ESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 5-223 4.95e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 118.41  E-value: 4.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQF-DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG----KRNFG 79
Cdd:PRK13636    6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQS--YALFpNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILL 157
Cdd:PRK13636   86 MVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 158 LDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK13636  165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 20-193 1.27e-30

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 114.97  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP-------GKRNfgmvfqsyALFPNLT 92
Cdd:PRK13539   18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylGHRN--------AMKPALT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGlkAKKYGKAEVK-EKALSALELVDLLNVKDKYpaqMSGGQQQRVALARALALSPDILLLDEPLSALDAKVRE 171
Cdd:PRK13539   90 VAENLEFW--AAFLGGEELDiAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164

                         170       180
                  ....*....|....*....|..
gi 1003869982 172 KLRREMRDLQEKVGvTTIMVTH 193
Cdd:PRK13539  165 LFAELIRAHLAQGG-IVIAATH 185
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 15-194 2.34e-30

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: 120.54  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLT 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIeyglkakKYGKAEVKEKALS-ALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:TIGR02868 425 VRENL-------RLARPDATDEELWaALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEkvGVTTIMVTHD 194
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 1-220 3.34e-30

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 119.77  E-value: 3.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-RNFG 79
Cdd:PRK15439    8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKaHQLG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 --MVFQSYALFPNLTALENIEYGLKAKKYGKAEVKekalsalELVDLLNVKDKYPAQMSG---GQQQRVALARALALSPD 154
Cdd:PRK15439   88 iyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMK-------QLLAALGCQLDLDSSAGSlevADRQIVEILRGLMRDSR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM--------------NHAEIMQIGTPE 220
Cdd:PRK15439  161 ILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMrdgtialsgktadlSTDDIIQAITPA 239
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
19-226 5.51e-30

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 114.89  E-value: 5.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN--FGMVFQ--SYALFPNLTAL 94
Cdd:PRK15112   28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQRIS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLKAKKYGKAEVKEKAL-SALELVDLL-NVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:PRK15112  108 QILDFPLRLNTDLEPEQREKQIiETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 173 LRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK15112  188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 18-222 5.79e-30

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 118.98  E-value: 5.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK-RNFGMVF-----QSYALFPNL 91
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipedrLGRGLVPDM 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENI---EYGLKA-KKYG---KAEVKEKalsALELVDLLNVK---DKYPA-QMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG3845   352 SVAENLilgRYRRPPfSRGGfldRKAIRAF---AEELIEEFDVRtpgPDTPArSLSGGNQQKVILARELSRDPKLLIAAQ 428

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG3845   429 PTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 1-230 7.09e-30

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 114.64  E-value: 7.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK-----DITALPPGK 75
Cdd:PRK11701    3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  76 RNF------GMVFQSYA--LFPNLTALENIEYGLKA---KKYGkaEVKEKALSALELVDL-LNVKDKYPAQMSGGQQQRV 143
Cdd:PRK11701   83 RRRllrtewGFVHQHPRdgLRMQVSAGGNIGERLMAvgaRHYG--DIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 144 ALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIY 223
Cdd:PRK11701  161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240


                  ....*..
gi 1003869982 224 QRPANPF 230
Cdd:PRK11701  241 DDPQHPY 247
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 14-239 7.54e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 114.81  E-value: 7.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTG-----SIAVNGKDI---TALPPGKRNFGMVFQSY 85
Cdd:PRK14271   31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 ALFPnLTALENIEYGLKAKKY-GKAEVKEKALSALELVDLLN-VKDKY---PAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:PRK14271  111 NPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDaVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvgVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVADFIGSIN 239
Cdd:PRK14271  190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS 266
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 18-230 1.28e-29

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 118.79  E-value: 1.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEeATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALE 95
Cdd:PRK11174  364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswRKHLSWVGQNPQLPHG-TLRD 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIeyglkakKYGKAEVKEKAL-SALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK11174  442 NV-------LLGNPDASDEQLqQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 164 ALDA----KVREKLRREMRdlqekvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPaNPF 230
Cdd:PRK11174  515 SLDAhseqLVMQALNAASR------RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLF 577
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 20-226 2.63e-29

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 118.29  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALENI 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLF-SGSVRENI 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKakKYGKAEVKEKALSALELVDLLNVKDKYP-------AQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVr 170
Cdd:TIGR00958 576 AYGLT--DTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC- 652

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 171 EKLRREMRDLQEKvgvTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:TIGR00958 653 EQLLQESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 18-230 2.78e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 114.44  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEA---TTGSIAVNGKDITALPPGKRN------FGMVFQS--YA 86
Cdd:PRK09473   30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNklraeqISMIFQDpmTS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENI-EYGLKAKKYGKAEVKEKALSALELVDLLNVKDK---YPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:PRK09473  110 LNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 163 SALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK09473  190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 20-213 3.65e-29

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: 111.59  E-value: 3.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE---ATTGSIAVNGKditALPPG--KRNFGMVFQSYALFPNLTAL 94
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPDqfQKCVAYVRQDDILLPGLTVR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYG----LKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:cd03234   100 ETLTYTailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 171 EKLRREMRDLQEKvGVTTIMVTHD-QEEALTMADKIVVMNHAEI 213
Cdd:cd03234   180 LNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 19-225 4.21e-29

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 117.12  E-value: 4.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFpNLTALEN 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVALVSQDVVLF-NDTIANN 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGlKAKKYGKAEVKEKALSA--LELVDLL------NVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:TIGR02203 426 IAYG-RTEQADRAEIERALAAAyaQDFVDKLplgldtPIGEN-GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 169 ----VREKLRREMRdlqekvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:TIGR02203 504 serlVQAALERLMQ------GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 5-235 4.23e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 112.44  E-value: 4.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEaTTGSIAVNGK-------------DITAL 71
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniyerrvNLNRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  72 ppgKRNFGMVFQSYALFPnLTALENIEYGLKAKKY-GKAEVK---EKALSALELVDLLNVK-DKYPAQMSGGQQQRVALA 146
Cdd:PRK14258   87 ---RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDdivESALKDADLWDEIKHKiHKSALDLSGGQQQRLCIA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 147 RALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVM--NHAEIMQI---GTPEE 221
Cdd:PRK14258  163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKK 242

                         250
                  ....*....|....
gi 1003869982 222 IYQRPANPFVADFI 235
Cdd:PRK14258  243 IFNSPHDSRTREYV 256
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
22-193 5.99e-29

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 110.28  E-value: 5.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPgkrnfgmVFQSYALF--------PNLTA 93
Cdd:PRK13538   19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-------EYHQDLLYlghqpgikTELTA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYGLKAKKYGKAEVkekALSALELVDLLNVKDKYPAQMSGGQQQRVALARaLALSPDIL-LLDEPLSALDAKVREK 172
Cdd:PRK13538   92 LENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQGVAR 167

                         170       180
                  ....*....|....*....|.
gi 1003869982 173 LRREMRDLQEKVGVtTIMVTH 193
Cdd:PRK13538  168 LEALLAQHAEQGGM-VILTTH 187
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-208 6.41e-29

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 116.42  E-value: 6.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP---GKRN 77
Cdd:PRK09700    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYG-LKAKKY------GKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALA 150
Cdd:PRK09700   82 IGIIYQELSVIDELTVLENLYIGrHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 151 LSPDILLLDEPLSALDAKVREKLRREMRDLQeKVGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:PRK09700  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVM 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-208 8.99e-29

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 109.63  E-value: 8.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPgkrnfgmvfQSYAL---FPn 90
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVP---------QRSEVpdsLP- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  91 LTALENIEYGLKAKKYG--------KAEVkEKALSALELVDLLNvkdKYPAQMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:NF040873   72 LTVRDLVAMGRWARRGLwrrltrddRAAV-DDALERVGLADLAG---RQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 163 SALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTmADKIVVM 208
Cdd:NF040873  148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 5-222 1.38e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 114.17  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVF 82
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEYGL---KAKKYGKAEVKEKAL-SALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLL 158
Cdd:PRK09536   84 QDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK09536  164 DEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 20-221 1.82e-28

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: 115.69  E-value: 1.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALENI 97
Cdd:COG5265   374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNI 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYG-LKAkkyGKAEVKEKALSA--LELVDLLnvKDKYPAQ-------MSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:COG5265   453 AYGrPDA---SEEEVEAAARAAqiHDFIESL--PDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 168 KVREKLRREMRDLQEkvGVTTIMVTH------DqeealtmADKIVVMNHAEIMQIGTPEE 221
Cdd:COG5265   528 RTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAE 578
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 20-193 2.38e-28

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 114.90  E-value: 2.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAvngkditaLPPGKRnfgMVF---QSYalFPNLTALEN 96
Cdd:COG4178   379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR---VLFlpqRPY--LPLGTLREA 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKAKKYGKAEVKEkalsALELVDL------LNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:COG4178   446 LLYPATAEAFSDAELRE----ALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521

                         170       180
                  ....*....|....*....|...
gi 1003869982 171 EKLRREMRdlQEKVGVTTIMVTH 193
Cdd:COG4178   522 AALYQLLR--EELPGTTVISVGH 542
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 5-222 3.37e-28

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 109.60  E-value: 3.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALP---PGKRNFGMV 81
Cdd:PRK10895    4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFPNLTALENIEYGLKAKKYGKAEV-KEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:PRK10895   84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK10895  164 PFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 15-193 4.72e-28

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: 107.83  E-value: 4.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQSYALFPNLTA 93
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYGLKAKKYGKAEVKEkalsALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:TIGR01189  91 LENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166

                         170       180
                  ....*....|....*....|
gi 1003869982 174 RREMRDLQEKVGVtTIMVTH 193
Cdd:TIGR01189 167 AGLLRAHLARGGI-VLLTTH 185
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
19-225 8.14e-28

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 113.52  E-value: 8.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALEN 96
Cdd:PRK13657  350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIEDN 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeyglkakKYGK-----AEVKEkALSALELVDLLNVK-DKYPA-------QMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK13657  429 I-------RVGRpdatdEEMRA-AAERAQAHDFIERKpDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEATS 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 164 ALDAKVREKLRREMRDLQEkvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK13657  501 ALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR 559
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 17-230 1.01e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 110.22  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE----ATTGSIAVNGKDITALPPGKR------NFGMVFQS-- 84
Cdd:PRK11022   20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGLKAKKYG-KAEVKEKALSALELV---DLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:PRK11022  100 TSLNPCYTVGFQIMEAIKVHQGGnKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PRK11022  180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 5-217 2.52e-27

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: 105.47  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFD--AFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN-FGMV 81
Cdd:cd03247     1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSYALFpNLTALENIeyglkakkyGKaevkekalsalelvdllnvkdkypaQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:cd03247    81 NQRPYLF-DTTLRNNL---------GR-------------------------RFSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 162 LSALDAKV-REKLRREMRDLQEKvgvTTIMVTHdQEEALTMADKIVVMNHAEIMQIG 217
Cdd:cd03247   126 TVGLDPITeRQLLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 20-222 4.32e-27

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 106.85  E-value: 4.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATtGSIAVNGKDITALPPG----KRN---------FGM-VFQSY 85
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAelarHRAylsqqqsppFAMpVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 ALF-PNLTALENIEyglkakkygkaevkeKALSalELVDLLNVKDKYP---AQMSGGQQQRVALARAL-----ALSPD-- 154
Cdd:COG4138    91 ALHqPAGASSEAVE---------------QLLA--QLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgq 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 155 ILLLDEPLSALDakVRE-----KLRREMRDLqekvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:COG4138   154 LLLLDEPMNSLD--VAQqaaldRLLRELCQQ----GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
10-222 6.48e-27

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 108.38  E-value: 6.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALP-PGKRNFGMVFQSYALF 88
Cdd:PRK13536   47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArLARARIGVVPQFDNLD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  89 PNLTALENI-----EYGLKAKkygkaEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK13536  127 LEFTVRENLlvfgrYFGMSTR-----EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK13536  202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 1-281 7.51e-27

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 110.40  E-value: 7.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEY-LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT--GSIAVNGKDITAlppgkRN 77
Cdd:PRK13549    1 MMEYlLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQA-----SN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 F------GMV--FQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVkDKYPA----QMSGGQQQRVAL 145
Cdd:PRK13549   76 IrdteraGIAiiHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKL-DINPAtpvgNLGLGQQQLVEI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 146 ARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEimQIGTpeeiyqR 225
Cdd:PRK13549  155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGT------R 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 226 PANPFVADFIGSI-------NFFSKnnEEHAI-----RPEHVTV--VQNNGMKtIVESMEFrgSVYRTEV 281
Cdd:PRK13549  226 PAAGMTEDDIITMmvgreltALYPR--EPHTIgevilEVRNLTAwdPVNPHIK-RVDDVSF--SLRRGEI 290
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 5-210 8.70e-27

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: 102.91  E-value: 8.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGkditalppgkrnfgmvfqs 84
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 yalfpnltalenieyglkakkygkaevkekalsalelvdllNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03221    62 -----------------------------------------TVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 165 LDAKVREKLRREMRDLQekvGvTTIMVTHDQEEALTMADKIVVMNH 210
Cdd:cd03221   101 LDLESIEALEEALKEYP---G-TVILVSHDRYFLDQVATKIIELED 142
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 19-221 1.29e-26

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 109.91  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFpNLTALEN 96
Cdd:PRK11160  355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVVSQRVHLF-SATLRDN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeygLKAKKYGKAEVKEKALSALELVDLLNVKDKYPA-------QMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:PRK11160  434 L---LLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 170 reklRREMRDLQEKV--GVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEE 221
Cdd:PRK11160  511 ----ERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQE 559
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 20-213 4.25e-26

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 103.70  E-value: 4.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALENI 97
Cdd:cd03248    30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKAKKYGKaeVKEKA--------LSALELVDLLNVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:cd03248   109 AYGLQSCSFEC--VKEAAqkahahsfISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 170 REKLRREMRDLQEKvgvTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03248   186 EQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 5-225 4.86e-26

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 107.97  E-value: 4.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE--EATTGSIAVN-------------GKDIT 69
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  70 ALPP-----------------------GKRNFGMVFQSYALFPNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLLN 126
Cdd:TIGR03269  81 PCPVcggtlepeevdfwnlsdklrrriRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 127 VKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIV 206
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240

                         250
                  ....*....|....*....
gi 1003869982 207 VMNHAEIMQIGTPEEIYQR 225
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV 259
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-207 6.22e-26

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 107.69  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT------ALPPG 74
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 krnFGMVFQSYALFPNLTALENIEYGLKAKKYG---KAEVKEKALSALELVDL---LNVKDKYpaqMSGGQQQRVALARA 148
Cdd:PRK11288   81 ---VAIIYQELHLVPEMTVAENLYLGQLPHKGGivnRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 149 LALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVV 207
Cdd:PRK11288  155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 5-220 9.99e-26

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: 101.83  E-value: 9.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE--EATTGSIAVNGKDITALPP---GKRNFG 79
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPeerARLGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPnltalenieyGLKAKKYgkaevkekalsalelvdLLNVKDKYpaqmSGGQQQRVALARALALSPDILLLD 159
Cdd:cd03217    81 LAFQYPPEIP----------GVKNADF-----------------LRYVNEGF----SGGEKKRNEILQLLLLEPDLAILD 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 160 EPLSALD-------AKVREKLRREmrdlqekvGVTTIMVTHDQEEALTM-ADKIVVMNHAEIMQIGTPE 220
Cdd:cd03217   130 EPDSGLDidalrlvAEVINKLREE--------GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 19-219 2.87e-25

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: 101.03  E-value: 2.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFP-----NL 91
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSgtirsNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALEnieyglkakKYGKAEVkekaLSALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:cd03244    99 DPFG---------EYSDEEL----WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDE 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 161 PLSALD----AKVREKLRREMRDlqekvgVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTP 219
Cdd:cd03244   166 ATASVDpetdALIQKTIREAFKD------CTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-219 3.11e-25

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 106.64  E-value: 3.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-TALPPGKRNFGMVFQSYALFPNLTALENI 97
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EY--GLKAKKYGKAEVKEKALsaLELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVreklRR 175
Cdd:TIGR01257 1025 LFyaQLKGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS----RR 1098

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1003869982  176 EMRD--LQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTP 219
Cdd:TIGR01257 1099 SIWDllLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-222 5.84e-25

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 5.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   8 QHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI-----AVNGKDITAlppgKRNFGMVF 82
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT----RRRVGYMS 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIEygLKAKKYG--KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:NF033858  346 QAFSLYGELTVRQNLE--LHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTmADKIVVMnHA-EIMQIGTPEEI 222
Cdd:NF033858  424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLM-HAgRVLASDTPAAL 484
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
18-226 3.49e-24

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 102.87  E-value: 3.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSYALFPNLTAlE 95
Cdd:PRK10789  329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSDTVA-N 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIEYGLKAKKygKAEVKEKALSALELVDLLNVKDKYPAQ-------MSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:PRK10789  408 NIALGRPDAT--QQEIEHVARLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 169 VREKLRREMRDLQEKvgvTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PRK10789  486 TEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 19-222 3.85e-24

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: 103.28  E-value: 3.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNlTALEN 96
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYLPQEPYIFSG-SILEN 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKAKKygkaeVKEKALSALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:TIGR01193 568 LLLGAKENV-----SQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNL 642

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 166 DAKVREKLRREMRDLQEKvgvTTIMVTHDQEEAlTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 5-230 5.11e-24

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 102.63  E-value: 5.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAftaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIA---------------------- 62
Cdd:PRK10261   20 IAFMQEQQKIAA---VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvielseqsaa 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  63 ----VNGKDItalppgkrnfGMVFQS--YALFPNLTALENIEYGLKAKK-YGKAEVKEKALSALELVDLLNVK---DKYP 132
Cdd:PRK10261   97 qmrhVRGADM----------AMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 133 AQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAE 212
Cdd:PRK10261  167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246

                         250
                  ....*....|....*...
gi 1003869982 213 IMQIGTPEEIYQRPANPF 230
Cdd:PRK10261  247 AVETGSVEQIFHAPQHPY 264
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 15-193 5.36e-24

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: 97.18  E-value: 5.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK-DITALPPGKRNFGMVFQSYALFPNLTA 93
Cdd:cd03231    11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYglkakkYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:cd03231    91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164

                         170       180
                  ....*....|....*....|
gi 1003869982 174 RREMRDLQEKVGVtTIMVTH 193
Cdd:cd03231   165 AEAMAGHCARGGM-VVLTTH 183
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 20-220 7.66e-24

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.83  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE--EATTGSIAVNGKDITALPPGKR---NFGMVFQSYALFPNLTAL 94
Cdd:COG0396    16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLKAKKYGK---AEVKEKALSALELVDL--------LNVKdkypaqMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:COG0396    96 NFLRTALNARRGEElsaREFLKLLKEKMKELGLdedfldryVNEG------FSGGEKKRNEILQMLLLEPKLAILDETDS 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 164 ALD-------AKVREKLRREmrdlqekvGVTTIMVTHdQEEALTM--ADKIVVMNHAEIMQIGTPE 220
Cdd:COG0396   170 GLDidalrivAEGVNKLRSP--------DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGKE 226
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 5-218 9.94e-24

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: 101.44  E-value: 9.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT--GSIAVNGKDITA---LPPGKRNFG 79
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKAsniRDTERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENI----EYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYP-AQMSGGQQQRVALARALALSPD 154
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 155 ILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEimQIGT 218
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-234 1.12e-23

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 97.49  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIavngkditaLPPGKRNFGM 80
Cdd:PRK09544    1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 VFQSYALFPNLTalenieygLKAKKYG--KAEVKEK-ALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILL 157
Cdd:PRK09544   72 VPQKLYLDTTLP--------LTVNRFLrlRPGTKKEdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 158 LDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHaEIMQIGTPEEIYQRPAnpFVADF 234
Cdd:PRK09544  144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE--FISMF 217
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-214 2.54e-23

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 96.49  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK---RN 77
Cdd:PRK11614    2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYGlkakkyGKAEVKEKALSALELV-----DLLNVKDKYPAQMSGGQQQRVALARALALS 152
Cdd:PRK11614   82 VAIVPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIM 214
Cdd:PRK11614  156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
19-222 9.22e-23

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 98.94  E-value: 9.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFpNLTALEN 96
Cdd:PRK11176  358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLF-NDTIANN 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKaKKYGKAEVKE--KALSALELVD-----LLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:PRK11176  437 IAYART-EQYSREQIEEaaRMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 170 REKLRREMRDLQEKvgvTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK11176  516 ERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 20-193 1.91e-22

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: 91.83  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAvngkditaLPPGKRNFGMVFQSYalFPNLTaleniey 99
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEGEDLLFLPQRPY--LPLGT------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 100 glkakkygkaevkekalsaleLVDLLNvkdkYPAQM--SGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREM 177
Cdd:cd03223    80 ---------------------LREQLI----YPWDDvlSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134

                         170
                  ....*....|....*.
gi 1003869982 178 RDLqekvGVTTIMVTH 193
Cdd:cd03223   135 KEL----GITVISVGH 146
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
21-222 3.08e-22

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 97.16  E-value: 3.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  21 KDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP---GKRNFGMVFQSY---ALFPNLTAL 94
Cdd:PRK09700  280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITESRrdnGFFPNFSIA 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 EN--IEYGLKAKKYGKA-----EVKEKALsALELVDLLNVK----DKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK09700  360 QNmaISRSLKDGGYKGAmglfhEVDEQRT-AENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 164 ALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQI------GTPEEI 222
Cdd:PRK09700  439 GIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQIltnrddMSEEEI 502
hmuV PRK13547
heme ABC transporter ATP-binding protein;
5-227 3.47e-22

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 94.12  E-value: 3.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAG-LEE-------ATTGSIAVNGKDITALPP--- 73
Cdd:PRK13547    2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGggaprgaRVTGDVTLNGEPLAAIDAprl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  74 GKRNFGMVFQSYALFPnLTALENIEYGL--KAKKYGKAEVKEK--ALSALELVDLLNVKDKYPAQMSGGQQQRVALARAL 149
Cdd:PRK13547   82 ARLRAVLPQAAQPAFA-FSAREIVLLGRypHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 150 A-LSPD--------ILLLDEPLSALDAKVREKLRREMRDLQE--KVGVTTIMvtHDQEEALTMADKIVVMNHAEIMQIGT 218
Cdd:PRK13547  161 AqLWPPhdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIV--HDPNLAARHADRIAMLADGAIVAHGA 238


                  ....*....
gi 1003869982 219 PEEIYqRPA 227
Cdd:PRK13547  239 PADVL-TPA 246
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 21-213 4.79e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 96.66  E-value: 4.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  21 KDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-NFGMVF-----QSYALF---P-- 89
Cdd:PRK15439  280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYldaPla 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  90 -NLTALENIEYGLKAKKYGKAEVKEKALSAlelvdlLNVKDKYPAQ----MSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK15439  360 wNVCALTHNRRGFWIKPARENAVLERYRRA------LNIKFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 165 LDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK15439  434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 17-196 6.75e-22

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 91.94  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDItalppgkrNFGmvfqsyalfPNLTALEN 96
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN--------QFG---------REASLIDA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IeyglkAKKYGKAEVKEkALSALELVDLLNVKDKYpAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRRE 176
Cdd:COG2401   106 I-----GRKGDFKDAVE-LLNAVGLSDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178

                         170       180
                  ....*....|....*....|
gi 1003869982 177 MRDLQEKVGVTTIMVTHDQE 196
Cdd:COG2401   179 LQKLARRAGITLVVATHHYD 198
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 20-235 1.53e-21

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 95.11  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT---GSIAVNGKDITAlPPGKRNFGMVFQSYALFPNLTALEN 96
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDA-KEMRAISAYVQQDDLFIPTLTVREH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEY------GLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQM---SGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:TIGR00955 120 LMFqahlrmPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVkglSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 168 KVREKLRREMRDLQEKvGVTTIMVTHD-QEEALTMADKIVVMNHAEIMQIGTPEEI--------YQRPANPFVADFI 235
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNPADFY 275
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
14-222 1.58e-21

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 91.97  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  14 FDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFPNL 91
Cdd:PRK10253   17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATTPGDI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 TALENIEYGLKAKK----YGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:PRK10253   97 TVQELVARGRYPHQplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 168 KVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK10253  177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 23-222 1.70e-21

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 91.53  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  23 ISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAtTGSIAVNGKDITALPPGK----RN---------FGM-VFQSYALF 88
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  89 -PNLTALENIeyglkakkygkaevkEKALSalELVDLLNVKDKYP---AQMSGGQQQRVALARA-LALSPDI------LL 157
Cdd:PRK03695   94 qPDKTRTEAV---------------ASALN--EVAEALGLDDKLGrsvNQLSGGEWQRVRLAAVvLQVWPDInpagqlLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 158 LDEPLSALD---AKVREKLRREMRDLqekvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK03695  157 LDEPMNSLDvaqQAALDRLLSELCQQ----GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 21-229 2.81e-21

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 91.30  E-value: 2.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  21 KDISFTVKKNEFVCLLGPSGCGKT----TLLRIL-AGLEeATTGSIAVNGKDITALPPGKRNFGMVFQS--YALFPNLT- 92
Cdd:PRK10418   20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVR-QTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTm 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:PRK10418   99 HTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 173 LRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANP 229
Cdd:PRK10418  179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 19-219 3.90e-21

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: 89.78  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGK--RNFGMVFQSYALFPNlTALEN 96
Cdd:cd03369    23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRSN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 I----EYGlKAKKYGKAEVKEKALSalelvdllnvkdkypaqMSGGQQQRVALARALALSPDILLLDEPLSAL----DAK 168
Cdd:cd03369   102 LdpfdEYS-DEEIYGALRVSEGGLN-----------------LSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDAL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 169 VREKLRREMRDlqekvgvTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTP 219
Cdd:cd03369   164 IQKTIREEFTN-------STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 20-249 4.96e-21

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: 94.24  E-value: 4.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKdiTALPPGKrnfgmvfqsyALFPNLTALENIEY 99
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ----------AWIQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  100 G--LKAKKYgKAEVKEKALSA-LELV---DLLNVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR--- 170
Cdd:TIGR00957  722 GkaLNEKYY-QQVLEACALLPdLEILpsgDRTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhi 799

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  171 -EKLRREMRDLQEKvgvTTIMVTHDQeEALTMADKIVVMNHAEIMQIGTPEEIYQRpaNPFVADFIgsINFFSKNNEEHA 249
Cdd:TIGR00957  800 fEHVIGPEGVLKNK---TRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQR--DGAFAEFL--RTYAPDEQQGHL 871
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
23-166 7.24e-21

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 89.14  E-value: 7.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  23 ISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAlppGKRNFGMVFQSY--ALFPNLTALENIEY- 99
Cdd:PRK13543   30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHlpGLKADLSTLENLHFl 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 100 -GLKAKKygkaeVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARaLALSPDIL-LLDEPLSALD 166
Cdd:PRK13543  107 cGLHGRR-----AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 5-207 9.79e-21

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 92.82  E-value: 9.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVnGKDItalppgkrNFGMVFQS 84
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------KIGYFDQH 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALF-PNLTALENIeyglkakKYGKAEVKEKALSALeLVDLL---NVKDKYPAQMSGGQQQRVALARALALSPDILLLDE 160
Cdd:COG0488   387 QEELdPDKTVLDEL-------RDGAPGGTEQEVRGY-LGRFLfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 161 PLSALDAKVREKLrrEMRdLQEKVGvTTIMVTHDQE--EALtmADKIVV 207
Cdd:COG0488   459 PTNHLDIETLEAL--EEA-LDDFPG-TVLLVSHDRYflDRV--ATRILE 501
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
20-225 2.77e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.91  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG----KRNFGMVFQSYALFPNLTALE 95
Cdd:PRK13638   17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVATVFQDPEQQIFYTDID 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 -NIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKyPAQ-MSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:PRK13638   97 sDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 174 RREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK13638  176 IAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
18-208 3.43e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 88.40  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT-ALppgKRNF-GMVFQSYAL---FPNLt 92
Cdd:PRK15056   21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqAL---QKNLvAYVPQSEEVdwsFPVL- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 alenIEYGLKAKKYG--------KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:PRK15056   97 ----VEDVVMMGRYGhmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1003869982 165 LDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:PRK15056  173 VDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV 215
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 19-213 4.19e-20

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 90.80  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQSYALFPNLTALEN 96
Cdd:PRK10522  338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQLLGPEG 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEyglkakkyGKAEVKEKALSALELVDLLNVKDKYPA--QMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLR 174
Cdd:PRK10522  418 KP--------ANPALVEKWLERLKMAHKLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1003869982 175 REMRDLQEKVGVTTIMVTHDqEEALTMADKIVVMNHAEI 213
Cdd:PRK10522  490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 5-230 4.20e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 90.92  E-value: 4.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHI----QKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKT-TLLRILAGLE----EATTGSIAVNGKDIT-ALPPG 74
Cdd:PRK15134    6 LAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvVYPSGDIRFHGESLLhASEQT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 KR-----NFGMVFQSYALfpNLTALENIEYGLkakkygkAEV--------KEKA----LSALELVDLLNVKDK---YPAQ 134
Cdd:PRK15134   86 LRgvrgnKIAMIFQEPMV--SLNPLHTLEKQL-------YEVlslhrgmrREAArgeiLNCLDRVGIRQAAKRltdYPHQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 135 MSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIM 214
Cdd:PRK15134  157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236

                         250
                  ....*....|....*.
gi 1003869982 215 QIGTPEEIYQRPANPF 230
Cdd:PRK15134  237 EQNRAATLFSAPTHPY 252
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-213 2.41e-19

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 88.52  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPP--GKRNfGMVFQSY-----ALFPNLT 92
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdGLAN-GIVYISEdrkrdGLVLGMS 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEygLKA-----KKYGKAEVKEKALSALELVDLLNVK----DKYPAQMSGGQQQRVALARALALSPDILLLDEPLS 163
Cdd:PRK10762  347 VKENMS--LTAlryfsRAGGSLKHADEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 164 ALD--AKvreklrREMRDLQEKV---GVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK10762  425 GVDvgAK------KEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 20-194 6.60e-19

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: 87.30  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSiavngkditALPPGKRNFGMVFQSYALFPNLTALENIEY 99
Cdd:TIGR03719  21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---------ARPQPGIKVGYLPQEPQLDPTKTVRENVEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 100 GLKAKK------------YG------------KAEVKEK---------------ALSALELVDllnvKDKYPAQMSGGQQ 140
Cdd:TIGR03719  92 GVAEIKdaldrfneisakYAepdadfdklaaeQAELQEIidaadawdldsqleiAMDALRCPP----WDADVTKLSGGER 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 141 QRVALARALALSPDILLLDEPLSALDAKVREKLRREmrdLQEKVGvTTIMVTHD 194
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPG-TVVAVTHD 217
PLN03211 PLN03211
ABC transporter G-25; Provisional
 12-217 1.79e-18

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 86.09  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  12 KQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAT--TGSIAVNGKDITAlpPGKRNFGMVFQSYALFP 89
Cdd:PLN03211   76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK--QILKRTGFVTQDDILYP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  90 NLTALENIEYGLKAK------KYGKAEVKEKALSALELVDLLN--VKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:PLN03211  154 HLTVRETLVFCSLLRlpksltKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKvGVTTIMVTHD-QEEALTMADKIVVMNHAEIMQIG 217
Cdd:PLN03211  234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 20-180 2.45e-18

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: 81.52  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEA--TTGSIAVNGKditalpPGKRNF----GMVFQSYALFPNLTA 93
Cdd:cd03232    23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR------PLDKNFqrstGYVEQQDVHSPNLTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LENIEYglkakkygkaevkekalSALeLVDLlnvkdkypaqmSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:cd03232    97 REALRF-----------------SAL-LRGL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147


                  ....*..
gi 1003869982 174 RREMRDL 180
Cdd:cd03232   148 VRFLKKL 154
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-194 4.30e-18

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: 84.99  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVnGKDItalppgkrNFGMVFQS 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQS 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 Y-ALFPNLTALENIEYGLKAKKYGKAEVKEKAlsaleLVDLLNVK----DKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1003869982 160 EPLSALDAkvrEKLRREMRDLQEKVGvTTIMVTHD 194
Cdd:TIGR03719 469 EPTNDLDV---ETLRALEEALLNFAG-CAVVISHD 499
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-207 6.18e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 6.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATT--GSIAVNG-----KDITAlppgKRN 77
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD----SEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVF--QSYALFPNLTALENIEYGLKAKKYG---KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALS 152
Cdd:NF040905   78 LGIVIihQELALIPYLSIAENIFLGNERAKRGvidWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 153 PDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVV 207
Cdd:NF040905  158 VKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITV 211
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 21-212 1.00e-17

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 84.31  E-value: 1.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   21 KDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG----KDITaLPPGKRNFGMVFQSYALFPN------ 90
Cdd:PTZ00265   402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVSQDPLLFSNsiknni 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   91 ---LTALENIEY--------------------GLKAKKYGKAEVKEKALSALELV------------DLLNVK------- 128
Cdd:PTZ00265   481 kysLYSLKDLEAlsnyynedgndsqenknkrnSCRAKCAGDLNDMSNTTDSNELIemrknyqtikdsEVVDVSkkvlihd 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  129 ------DKY-------PAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHdQ 195
Cdd:PTZ00265   561 fvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-R 639

                          250
                   ....*....|....*..
gi 1003869982  196 EEALTMADKIVVMNHAE 212
Cdd:PTZ00265   640 LSTIRYANTIFVLSNRE 656
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
5-244 1.23e-17

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 82.26  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQhIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE----ATTGSIAVNGKDITALPPGKR---- 76
Cdd:COG4170     9 LTIE-IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkii 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  77 --NFGMVFQ--SYALFPNLTALENIEYGLKAKKYG------KAEVKEKALSALELVDLLNVKD---KYPAQMSGGQQQRV 143
Cdd:COG4170    88 grEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 144 ALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIY 223
Cdd:COG4170   168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247

                         250       260
                  ....*....|....*....|.
gi 1003869982 224 QRPANPFVADFIGSINFFSKN 244
Cdd:COG4170   248 KSPHHPYTKALLRSMPDFRQP 268
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
20-225 1.41e-17

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 83.61  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG--KRNFGMVFQ-----SYALFPNLT 92
Cdd:PRK10790  357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQdpvvlADTFLANVT 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEyglkakkygkaevKEKALSALELVDLLNVKDKYPA-----------QMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:PRK10790  437 LGRDIS-------------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEA 503

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 162 LSALDAKVREKLRREMRDLQEKvgvTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK10790  504 TANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
23-213 1.98e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 82.65  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  23 ISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKR-NFGMVF-----QSYALFPNLTALEN 96
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiRAGIMLcpedrKAEGIIPVHSVADN 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  97 IEYGLKaKKYGKA-----EVKEKALsALELVDLLNVKDKYPAQ----MSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:PRK11288  352 INISAR-RHHLRAgclinNRWEAEN-ADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 168 KVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK11288  430 GAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
18-224 2.25e-17

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 80.60  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA----------------LPPGKrnfGMV 81
Cdd:PRK10575   25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafarkvaylpqqLPAAE---GMT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  82 FQSyalfpnLTALENIEYGLKAKKYGKAEvKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:PRK10575  102 VRE------LVAIGRYPWHGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 162 LSALD-AKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PRK10575  175 TSALDiAHQVDVLALVHRLSQER-GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 1-208 2.27e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 82.74  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   1 MSEYLSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPGKRN--- 77
Cdd:PRK10762    1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeag 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 FGMVFQSYALFPNLTALENIEYGL-KAKKYGKAEVKEKALSALELVDLLNVK---DKYPAQMSGGQQQRVALARALALSP 153
Cdd:PRK10762   81 IGIIHQELNLIPQLTIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLNLRfssDKLVGELSIGEQQMVEIAKVLSFES 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 154 DILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:PRK10762  161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVF 214
PLN03232 PLN03232
ABC transporter C family member; Provisional
 20-224 2.87e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 83.10  E-value: 2.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAG-LEEATTGSIAVNGKdiTALPPgkrnfgmvfQSYALFpNLTALENIE 98
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--VAYVP---------QVSWIF-NATVRENIL 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   99 YG--LKAKKYGKAeVKEKALSA-LELV---DLLNVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV-RE 171
Cdd:PLN03232   701 FGsdFESERYWRA-IDVTALQHdLDLLpgrDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVaHQ 778

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982  172 KLRREMRDlqEKVGVTTIMVThDQEEALTMADKIVVMNHAEIMQIGTPEEIYQ 224
Cdd:PLN03232   779 VFDSCMKD--ELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-207 3.27e-17

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: 79.76  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  26 TVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPPG-KRNFGMVFQSYalfpnltaLENIEYGLKAK 104
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDL--------LSSITKDFYTH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 105 KYGKAEVkekaLSALELVDLLnvkDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKV 184
Cdd:cd03237    93 PYFKTEI----AKPLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165

                         170       180
                  ....*....|....*....|...
gi 1003869982 185 GVTTIMVTHDQEEALTMADKIVV 207
Cdd:cd03237   166 EKTAFVVEHDIIMIDYLADRLIV 188
PLN03130 PLN03130
ABC transporter C family member; Provisional
 20-222 5.00e-17

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 82.09  E-value: 5.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLR-ILAGLEEATTGSIAVNGKditalppgkrnFGMVFQSYALFpNLTALENIE 98
Cdd:PLN03130   633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNIL 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   99 YGL--KAKKYGKAeVKEKALSA-LELV---DLLNVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREK 172
Cdd:PLN03130   701 FGSpfDPERYERA-IDVTALQHdLDLLpggDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982  173 -----LRREMRdlqekvGVTTIMVThDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PLN03130   779 vfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 20-240 8.56e-17

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: 81.50  E-value: 8.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKdITALPpgkrnfgmvfQSYALFPNlTALENIEY 99
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP----------QTSWIMPG-TIKDNIIF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  100 GLKAKKYGKAEVKeKALSALELVDLLNVKDKYP-----AQMSGGQQQRVALARALALSPDILLLDEPLSALDAkVREKLR 174
Cdd:TIGR01271  510 GLSYDEYRYTSVI-KACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV-VTEKEI 587

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982  175 REMRDLQEKVGVTTIMVTHDQEEaLTMADKIVVMNHAEIMQIGTPEEIyQRPANPFVADFIGSINF 240
Cdd:TIGR01271  588 FESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLLGLEAF 651
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
10-207 2.30e-16

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 79.85  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIavnGKDIT-ALPPG--KRNFGMVFQSYa 86
Cdd:PRK13409  346 LTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKiSYKPQyiKPDYDGTVEDL- 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 lfpnltaLENIeyglkAKKYGKAEVKEKALSALELVDLLnvkDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK13409  421 -------LRSI-----TDDLGSSYYKSEIIKPLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1003869982 167 AKVREKLRREMRDLQEKVGVTTIMVTHDqeeaLTM----ADKIVV 207
Cdd:PRK13409  486 VEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMV 526
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 20-208 2.53e-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: 76.60  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI---AVNGKDITALPPGKRNFGMVfqSYA----LFPNLT 92
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSV--AYAaqkpWLLNAT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  93 ALENIEYGLKAKKYGKAEVKEkALSALELVDLLNVKDKYPA-----QMSGGQQQRVALARALALSPDILLLDEPLSALDA 167
Cdd:cd03290    95 VEENITFGSPFNKQRYKAVTD-ACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1003869982 168 KVREKLRRE--MRDLQEKvGVTTIMVTHdQEEALTMADKIVVM 208
Cdd:cd03290   174 HLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLPHADWIIAM 214
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 10-213 4.44e-16

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: 75.38  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGL---EEATTGSIAVNGKDIT-ALPPGKRNFGMVFQSY 85
Cdd:cd03233    13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKeFAEKYPGEIIYVSEED 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 ALFPNLTALENIEYGLKAKkyGKAEVKekalsalelvdllnvkdkypaQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:cd03233    93 VHFPTLTVRETLDFALRCK--GNEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 166 DAKVREKLRREMRDLQEKVGVTTIM-VTHDQEEALTMADKIVVMNHAEI 213
Cdd:cd03233   150 DSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 2-207 5.56e-16

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 78.67  E-value: 5.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   2 SEYLSIQHIQKQFDAFTaLKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSiaVNGKDITALPPG--KRNFG 79
Cdd:COG1245   339 ETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQyiSPDYD 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENieyglkakKYGKAEVKEKalsaLELVDLLnvkDKYPAQMSGGQQQRVALARALALSPDILLLD 159
Cdd:COG1245   416 GTVEEFLRSANTDDFGS--------SYYKTEIIKP----LGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLD 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003869982 160 EPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDqeeaLTM----ADKIVV 207
Cdd:COG1245   481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMV 528
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 58-222 8.85e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 78.53  E-value: 8.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   58 TGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFpNLTALENIEYGLKAKKYGKAEVKEKALSALELVDLL-NVKDK---- 130
Cdd:PTZ00265  1276 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpNKYDTnvgp 1354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  131 YPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHdQEEALTMADKIVVMNH 210
Cdd:PTZ00265  1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433

                          170
                   ....*....|....*..
gi 1003869982  211 AE-----IMQIGTPEEI 222
Cdd:PTZ00265  1434 PDrtgsfVQAHGTHEEL 1450
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 20-226 1.11e-15

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: 76.05  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKdITALPpgkrnfgmvfQSYALFPNlTALENIEY 99
Cdd:cd03291    53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS----------QFSWIMPG-TIKENIIF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 100 GLKAKKYGKAEVKeKALSALELVDLLNVKDKYP-----AQMSGGQQQRVALARALALSPDILLLDEPLSALDAkVREKLR 174
Cdd:cd03291   121 GVSYDEYRYKSVV-KACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV-FTEKEI 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 175 REMRDLQEKVGVTTIMVTHDQEEaLTMADKIVVMNHAEIMQIGT-PEEIYQRP 226
Cdd:cd03291   199 FESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTfSELQSLRP 250
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 22-213 1.64e-15

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 77.17  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGL-EEATTGSIAVNGKDITALPPGK---RNFGMVFQS---YALFPNLTAL 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEYGLKAKKYGKAEVKEKAL--SALELVDLLNVKDKYP----AQMSGGQQQRVALARALALSPDILLLDEPLSALDAK 168
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAElqIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1003869982 169 VREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 35-194 1.84e-15

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 77.08  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  35 LLGPSGCGKTTLLRILAGLEEATTGSiavngkdiTALPPGKRnFGMVFQSYALFPNLTALENIEYGLKAKK--------- 105
Cdd:PRK11819   38 VLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGIK-VGYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfnei 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 106 ---YGK------------AEVKEK---------------ALSALELVDllnvKDKYPAQMSGGQQQRVALARALALSPDI 155
Cdd:PRK11819  109 yaaYAEpdadfdalaaeqGELQEIidaadawdldsqleiAMDALRCPP----WDAKVTKLSGGERRRVALCRLLLEKPDM 184

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1003869982 156 LLLDEPLSALDAKVREKLRREmrdLQEKVGvTTIMVTHD 194
Cdd:PRK11819  185 LLLDEPTNHLDAESVAWLEQF---LHDYPG-TVVAVTHD 219
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 26-208 2.37e-15

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 76.75  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  26 TVKKNEFVCLLGPSGCGKTTLLRILAGLeeattgsiavngkditaLPPgkrNFGMV------------FQSYALFPNLTA 93
Cdd:COG1245    95 VPKKGKVTGILGPNGIGKSTALKILSGE-----------------LKP---NLGDYdeepswdevlkrFRGTELQDYFKK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  94 LEN--------IEYGLKAKKYGKAEVKE---------KALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDIL 156
Cdd:COG1245   155 LANgeikvahkPQYVDLIPKVFKGTVREllekvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003869982 157 LLDEPLSALDakVREKLR--REMRDLQEKvGVTTIMVTHDqeeaLT----MADKIVVM 208
Cdd:COG1245   235 FFDEPSSYLD--IYQRLNvaRLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 20-203 3.43e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 73.06  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA-LPPGKRNFGMVFQSYALFPNLTALENIE 98
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  99 YGLkakkygkaEVKEKALSALELVDLLNVKD--KYP-AQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRR 175
Cdd:PRK13540   97 YDI--------HFSPGAVGITELCRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168

                         170       180
                  ....*....|....*....|....*...
gi 1003869982 176 EMRDLQEKVGvtTIMVTHDQEEALTMAD 203
Cdd:PRK13540  169 KIQEHRAKGG--AVLLTSHQDLPLNKAD 194
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 22-213 3.81e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 76.12  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGL-EEATTGSIAVNGKDITALPPG---KRNFGMVFQS---YALFPNLTAL 94
Cdd:PRK13549  280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENIEygLKA-KKYGKAEVKEKAL---SALELVDLLNVKDKYP----AQMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PRK13549  360 KNIT--LAAlDRFTGGSRIDDAAelkTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1003869982 167 AKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:PRK13549  438 VGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PLN03232 PLN03232
ABC transporter C family member; Provisional
 20-245 5.19e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 76.17  E-value: 5.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFPNlTALENI 97
Cdd:PLN03232  1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLSIIPQSPVLFSG-TVRFNI 1330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EyglKAKKYGKAEVKEkalsALELVDLLNVKDKYP----AQM-------SGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PLN03232  1331 D---PFSEHNDADLWE----ALERAHIKDVIDRNPfgldAEVseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  167 AKVREKLRREMRdlqEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFV----------ADFIG 236
Cdd:PLN03232  1404 VRTDSLIQRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFrmvhstgpanAQYLS 1480


                   ....*....
gi 1003869982  237 SINFFSKNN 245
Cdd:PLN03232  1481 NLVFERREN 1489
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 10-208 1.05e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 74.77  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  10 IQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT------ALPPGkrnFGMVFQ 83
Cdd:PRK10982    4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskeALENG---ISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYALFPNLTALENIEYGLKAKK-----YGKAEVKEKALSAlELVDLLNVKDKYpAQMSGGQQQRVALARALALSPDILLL 158
Cdd:PRK10982   81 ELNLVLQRSVMDNMWLGRYPTKgmfvdQDKMYRDTKAIFD-ELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIM 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003869982 159 DEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVM 208
Cdd:PRK10982  159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
PTZ00243 PTZ00243
ABC transporter; Provisional
 20-226 1.40e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 74.82  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAvngkditalppGKRNFGMVFQSyALFPNLTALENIEY 99
Cdd:PTZ00243   676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  100 G--------LKAKKYGKAEVKEKALSA-LELvdllNVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVR 170
Cdd:PTZ00243   744 FdeedaarlADAVRVSQLEADLAQLGGgLET----EIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982  171 EKLRREMRdLQEKVGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEIYQRP 226
Cdd:PTZ00243   819 ERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
19-241 1.47e-14

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 73.30  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEE----ATTGSIAVNGKDITALPPGKR------NFGMVFQSyalf 88
Cdd:PRK15093   22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE---- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  89 PN--LTALENIEYGLKA-------KKYGKAEVKEKALSALELVDLLNVKD------KYPAQMSGGQQQRVALARALALSP 153
Cdd:PRK15093   98 PQscLDPSERVGRQLMQnipgwtyKGRWWQRFGWRKRRAIELLHRVGIKDhkdamrSFPYELTEGECQKVMIAIALANQP 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 154 DILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVAD 233
Cdd:PRK15093  178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257


                  ....*...
gi 1003869982 234 FIGSINFF 241
Cdd:PRK15093  258 LIRAIPDF 265
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
18-225 2.18e-14

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 74.01  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI------TALPP---------GKrNfgmvf 82
Cdd:NF033858   15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCPriaympqglGK-N----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 qsyaLFPNLTALENIE-----YGLkakkyGKAEVKEKALSALELVDLLNVKDKyPA-QMSGGQQQRVALARALALSPDIL 156
Cdd:NF033858   89 ----LYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 157 LLDE------PLSaldakvreklRREMRDL-----QEKVGVTTIMVTHDQEEALTMaDKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:NF033858  159 ILDEpttgvdPLS----------RRQFWELidrirAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 19-259 2.79e-14

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 73.89  E-value: 2.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI-TALPPGKRNFGMVFQSYALFPNLTALENI 97
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREM 177
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  178 RDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRPANPFVA---------DFIGSIN----FFSKN 244
Cdd:TIGR01257 2114 VSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVtmkikspkdDLLPDLNpveqFFQGN 2192

                          250
                   ....*....|....*
gi 1003869982  245 NEEHAIRPEHVTVVQ 259
Cdd:TIGR01257 2193 FPGSVQRERHYNMLQ 2207
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 19-222 4.54e-14

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 72.62  E-value: 4.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGkditalppgkrNFGMVFQSYALFPNLTALENIE 98
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  99 ygLKAKKYG--KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRRE 176
Cdd:PRK13545  108 --LKGLMMGltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 177 MRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PRK13545  186 MNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
PTZ00243 PTZ00243
ABC transporter; Provisional
 20-230 5.01e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 73.27  E-value: 5.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSYALFPNlTALENI 97
Cdd:PTZ00243  1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EYGLKAKkygKAEVkekaLSALELVDLlnvKDKYPAQMSG--------------GQQQRVALARALaLSPD--ILLLDEP 161
Cdd:PTZ00243  1405 DPFLEAS---SAEV----WAALELVGL---RERVASESEGidsrvleggsnysvGQRQLMCMARAL-LKKGsgFILMDEA 1473

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982  162 LSALDAKVReklrremRDLQEKV-----GVTTIMVTHDQEealTMA--DKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:PTZ00243  1474 TANIDPALD-------RQIQATVmsafsAYTVITIAHRLH---TVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 5-180 6.46e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 69.52  E-value: 6.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAfTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPpgKRNFGMVFQS 84
Cdd:PRK13541    2 LSLHQLQFNIEQ-KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  85 YALFPNLTALENIEYGlkAKKYGKAEVKEKALSALELVDLLnvkDKYPAQMSGGQQQRVALARALALSPDILLLDEplsa 164
Cdd:PRK13541   79 LGLKLEMTVFENLKFW--SEIYNSAETLYAAIHYFKLHDLL---DEKCYSLSSGMQKIVAIARLIACQSDLWLLDE---- 149

                         170
                  ....*....|....*.
gi 1003869982 165 ldakVREKLRREMRDL 180
Cdd:PRK13541  150 ----VETNLSKENRDL 161
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 8-166 6.67e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 72.07  E-value: 6.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   8 QHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVnGKDItalppgkrNFGMVFQSY-A 86
Cdd:PRK11819  328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQSRdA 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 LFPNLTALENIEYGLKAKKYGKAEVKEKA-LSAlelvdlLNVK----DKYPAQMSGGQQQRVALARALALSPDILLLDEP 161
Cdd:PRK11819  399 LDPNKTVWEEISGGLDIIKVGNREIPSRAyVGR------FNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472


                  ....*
gi 1003869982 162 LSALD 166
Cdd:PRK11819  473 TNDLD 477
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-213 1.52e-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: 67.01  E-value: 1.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   29 KNEFVCLLGPSGCGKTTLLRILAG-LEEATTGSIAVNGkditalppgkrnfgmvfqsyalfpnltalenieyglkakkyg 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------ 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  108 kaevkEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRD-----LQE 182
Cdd:smart00382  39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1003869982  183 KVGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 20-206 1.64e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 71.13  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITAL----PPgkRNF-GMVFQSYAlfpnltal 94
Cdd:PRK11147   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPP--RNVeGTVYDFVA-------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  95 ENI-EYGLKAKKYGKA------EVKEKALSAL----ELVDLLNV-----------------KDKYPAQMSGGQQQRVALA 146
Cdd:PRK11147   89 EGIeEQAEYLKRYHDIshlvetDPSEKNLNELaklqEQLDHHNLwqlenrinevlaqlgldPDAALSSLSGGWLRKAALG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 147 RALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVgvttIMVTHDQEEALTMADKIV 206
Cdd:PRK11147  169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRIV 224
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 19-224 3.45e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 70.14  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDI---TALPPGKRNFGMVFQ---SYALFPNL- 91
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTEerrSTGIYAYLd 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  92 ----TALENIE-----YGLKAKKYGKAEVKEkalsaleLVDLLNVKDkyPAQ------MSGGQQQRVALARALALSPDIL 156
Cdd:PRK10982  343 igfnSLISNIRnyknkVGLLDNSRMKSDTQW-------VIDSMRVKT--PGHrtqigsLSGGNQQKVIIGRWLLTQPEIL 413

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 157 LLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQI-----GTPEEIYQ 224
Cdd:PRK10982  414 MLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIvdtktTTQNEILR 485
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 5-220 3.48e-13

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 68.13  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE--EATTGSIAVNGKDITALPPGKRNFGMVF 82
Cdd:CHL00131    8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLGIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 QSYALFPNLTALENIE-----YGLKAKKYGKAEVK-----EKALSALELVDL------LNVKDKYpaqmSGGQQQRVALA 146
Cdd:CHL00131   88 LAFQYPIEIPGVSNADflrlaYNSKRKFQGLPELDpleflEIINEKLKLVGMdpsflsRNVNEGF----SGGEKKRNEIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 147 RALALSPDILLLDEPLSALD-------AKVREKLRRemrdlQEKvgvTTIMVTHDQEeaL---TMADKIVVMNHAEIMQI 216
Cdd:CHL00131  164 QMALLDSELAILDETDSGLDidalkiiAEGINKLMT-----SEN---SIILITHYQR--LldyIKPDYVHVMQNGKIIKT 233


                  ....
gi 1003869982 217 GTPE 220
Cdd:CHL00131  234 GDAE 237
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-208 3.85e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 69.84  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  26 TVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALppgKRNFGMVFQSYalFPNL-----TALENIEYG 100
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVL---KRFRGTELQNY--FKKLyngeiKVVHKPQYV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 101 LKAKKYGKAEVKE---------KALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDakVRE 171
Cdd:PRK13409  170 DLIPKVFKGKVREllkkvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQ 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1003869982 172 KLR--REMRDLQEKVGVttIMVTHDqeeaLT----MADKIVVM 208
Cdd:PRK13409  248 RLNvaRLIRELAEGKYV--LVVEHD----LAvldyLADNVHIA 284
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 23-208 4.82e-13

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 69.83  E-value: 4.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  23 ISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITA--LPPGKRNFGMVFQSYALFPNLTALENIEYG 100
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREAYRQLFSAVFSDFHLFDRLLGLDGEADP 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 101 LKAKKY-------GKAEVKEKALSALELvdllnvkdkypaqmSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKL 173
Cdd:COG4615   431 ARARELlerleldHKVSVEDGRFSTTDL--------------SQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVF 496

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1003869982 174 RREM-RDLQEKvGVTTIMVTHDqEEALTMADKIVVM 208
Cdd:COG4615   497 YTELlPELKAR-GKTVIAISHD-DRYFDLADRVLKM 530
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 7-196 5.57e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.59  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   7 IQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALppgkrnfgmvFQSY- 85
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY----------FDQHr 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  86 -ALFPNLTALENIeyglkakKYGKAEV-----KEKALSALElvDLL--------NVKdkypaQMSGGQQQRVALARaLAL 151
Cdd:PRK11147  392 aELDPEKTVMDNL-------AEGKQEVmvngrPRHVLGYLQ--DFLfhpkramtPVK-----ALSGGERNRLLLAR-LFL 456

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1003869982 152 SP-DILLLDEPLSALDAKVREKLRREMRDLQEkvgvTTIMVTHDQE 196
Cdd:PRK11147  457 KPsNLLILDEPTNDLDVETLELLEELLDSYQG----TVLLVSHDRQ 498
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
17-234 1.09e-12

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 67.15  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  17 FTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGK-DITALPPGkrnfgmvfqsyaLFPNLTALE 95
Cdd:PRK13546   37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAG------------LSGQLTGIE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIEYGLKAKKYGKAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRR 175
Cdd:PRK13546  105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 176 EMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQRpANPFVADF 234
Cdd:PRK13546  185 KIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDF 241
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 27-207 2.22e-12

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: 64.52  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  27 VKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALPpgkrnfgmvfqsyalfpnltalenieyglkakky 106
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP---------------------------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 107 gkaevkekalsalELVDLlnvkdkypaqmSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVGV 186
Cdd:cd03222    68 -------------QYIDL-----------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123

                         170       180
                  ....*....|....*....|.
gi 1003869982 187 TTIMVTHDQEEALTMADKIVV 207
Cdd:cd03222   124 TALVVEHDLAVLDYLSDRIHV 144
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 5-195 2.75e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 65.58  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE--EATTGSIAVNGKDITALPPGKR---NFG 79
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  80 MVFQSYALFPNLTALENIEYGLKA-KKYGKAEvkekALSALELVDLLNVKD---KYPAQM---------SGGQQQRVALA 146
Cdd:PRK09580   82 MAFQYPVEIPGVSNQFFLQTALNAvRSYRGQE----PLDRFDFQDLMEEKIallKMPEDLltrsvnvgfSGGEKKRNDIL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003869982 147 RALALSPDILLLDEPLSALD-------AKVREKLRREMRDLqekvgvttIMVTHDQ 195
Cdd:PRK09580  158 QMAVLEPELCILDESDSGLDidalkivADGVNSLRDGKRSF--------IIVTHYQ 205
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 18-215 1.18e-11

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: 64.11  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEaTTGSIAVNGKDITALPPGK--RNFGMVFQSYALFPNlTALE 95
Cdd:cd03289    18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-TFRK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  96 NIEyglkakKYGKAEvKEKALSALELVDLLNVKDKYPAQM-----------SGGQQQRVALARALALSPDILLLDEPLSA 164
Cdd:cd03289    96 NLD------PYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1003869982 165 LDAKVREKLRREMRdlQEKVGVTTIMVTHdQEEALTMADKIVVMNHAEIMQ 215
Cdd:cd03289   169 LDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 20-199 3.12e-11

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 64.55  E-value: 3.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEeATTGSIAVNGK--DITALPPGKRNFGMVFQSYALFPNlTALENI 97
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVswNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNL 1312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EyglKAKKYGKAEVKEKAlsalELVDLLNVKDKYPAQM-----------SGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:TIGR01271 1313 D---PYEQWSDEEIWKVA----EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1003869982  167 AKVREKLRREMRdlQEKVGVTTIMVTHDQEEAL 199
Cdd:TIGR01271 1386 PVTLQIIRKTLK--QSFSNCTVILSEHRVEALL 1416
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 22-193 4.26e-11

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 64.00  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  22 DISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVngkditalPPGKRNFGMVFQSYalFPNLTALENIEY-- 99
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAKGKLFYVPQRPY--MTLGTLRDQIIYpd 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 100 ---GLKAKKYGKAEVkEKALSALELVDLLN-------VKDkYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKV 169
Cdd:TIGR00954 540 sseDMKRRGLSDKDL-EQILDNVQLTHILEreggwsaVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617

                         170       180
                  ....*....|....*....|....
gi 1003869982 170 REKLRREMRDlqekVGVTTIMVTH 193
Cdd:TIGR00954 618 EGYMYRLCRE----FGITLFSVSH 637
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-194 5.99e-11

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: 62.00  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  26 TVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALppgkRNF-GMVFQSYalfpnLTALenIEYGLKAK 104
Cdd:cd03236    22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEIL----DEFrGSELQNY-----FTKL--LEGDVKVI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 105 KYGK------AEVKEKALSALELVDLLNVKDKYPAQM-------------SGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:cd03236    91 VKPQyvdlipKAVKGKVGELLKKKDERGKLDELVDQLelrhvldrnidqlSGGELQRVAIAAALARDADFYFFDEPSSYL 170

                         170       180
                  ....*....|....*....|....*....
gi 1003869982 166 DAKVREKLRREMRDLQEKvGVTTIMVTHD 194
Cdd:cd03236   171 DIKQRLNAARLIRELAED-DNYVLVVEHD 198
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 20-224 8.43e-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: 63.43  E-value: 8.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFPNLTALENI 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EYGlkakKYGKAEVkekaLSALELVDLLNVKDKYPAQM-----------SGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:TIGR00957 1382 PFS----QYSDEEV----WWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  167 AKVREKLRREMRDLQEKVGVTTImvTHDQEealTMAD--KIVVMNHAEIMQIGTPEEIYQ 224
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTI--AHRLN---TIMDytRVIVLDKGEVAEFGAPSNLLQ 1508
PLN03140 PLN03140
ABC transporter G family member; Provisional
 15-179 1.86e-10

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 62.17  E-value: 1.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   15 DAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGleEATTGSIAVNGKdITALPPGKRNF----GMVFQSYALFPN 90
Cdd:PLN03140   891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKQETFarisGYCEQNDIHSPQ 967

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   91 LTALENIEYG--LK-AKKYGKAEVKEKALSALELVDLLNVKDK---YPA--QMSGGQQQRVALARALALSPDILLLDEPL 162
Cdd:PLN03140   968 VTVRESLIYSafLRlPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047

                          170
                   ....*....|....*..
gi 1003869982  163 SALDAKVREKLRREMRD 179
Cdd:PLN03140  1048 SGLDARAAAIVMRTVRN 1064
PLN03130 PLN03130
ABC transporter C family member; Provisional
 20-222 2.85e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 61.68  E-value: 2.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDIT--ALPPGKRNFGMVFQSYALFPNltaleNI 97
Cdd:PLN03130  1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRKVLGIIPQAPVLFSG-----TV 1329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   98 EYGLKA-KKYGKAEVKEkalsALELVDLLNVKDKYP-----------AQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:PLN03130  1330 RFNLDPfNEHNDADLWE----SLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003869982  166 ----DAKVREKLRREMRdlqekvGVTTIMVTHdQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:PLN03130  1406 dvrtDALIQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
108-222 4.74e-10

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 108 KAEVKEKALSALELVDLLNVKDKYPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVT 187
Cdd:NF000106  118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1003869982 188 TIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEI 222
Cdd:NF000106  197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 20-202 1.88e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.97  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAglEEATTGSIA-----VNGKDITALPPgkRNFGMVFQSYALFPNLTAL 94
Cdd:TIGR00956  779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITggdrlVNGRPLDSSFQ--RSIGYVQQQDLHLPTSTVR 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   95 ENIEYGL------KAKKYGKAEVKEKALSALELVDL-----------LNVKdkypaqmsggQQQRVALARALALSPDILL 157
Cdd:TIGR00956  855 ESLRFSAylrqpkSVSKSEKMEYVEEVIKLLEMESYadavvgvpgegLNVE----------QRKRLTIGVELVAKPKLLL 924

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1003869982  158 -LDEPLSALDAKVREKLRREMRDLQeKVGvTTIMVTHDQEEALTMA 202
Cdd:TIGR00956  925 fLDEPTSGLDSQTAWSICKLMRKLA-DHG-QAILCTIHQPSAILFE 968
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 12-253 2.78e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   12 KQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILA----GLEEATTGSIAVNGKDITALPPGKRnfGMVFQSYAL 87
Cdd:TIGR00956   69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYR--GDVVYNAET 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   88 ---FPNLTALENIEY------------GLKAKKYGKaEVKEKALSALELVDLLNVK--DKYPAQMSGGQQQRVALARALA 150
Cdd:TIGR00956  147 dvhFPHLTVGETLDFaarcktpqnrpdGVSREEYAK-HIADVYMATYGLSHTRNTKvgNDFVRGVSGGERKRVSIAEASL 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  151 LSPDILLLDEPLSALDAKVREKLrreMRDLQEKVGV--TTIMVTHDQ--EEALTMADKIVVMNHAEIMQIGTPEEI---- 222
Cdd:TIGR00956  226 GGAKIQCWDNATRGLDSATALEF---IRALKTSANIldTTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGPADKAkqyf 302

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1003869982  223 ----YQRPANPFVADFIGSINffskNNEEHAIRPE 253
Cdd:TIGR00956  303 ekmgFKCPDRQTTADFLTSLT----SPAERQIKPG 333
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 19-210 3.04e-09

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: 55.41  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  19 ALKDISFTVKKNEFVCLLGPSGCGKTTLLriLAGLEEATTGSIAvngKDITALPPGKrnfgMVFQSyalfpNLTALenIE 98
Cdd:cd03238    10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLI---SFLPKFSRNK----LIFID-----QLQFL--ID 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  99 YGLKAKKYGKAevkekaLSALelvdllnvkdkypaqmSGGQQQRVALARALALSPD--ILLLDEPLSALDAKVREKLRRE 176
Cdd:cd03238    74 VGLGYLTLGQK------LSTL----------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1003869982 177 MRDLQEKvGVTTIMVTHDqEEALTMADKIVVMNH 210
Cdd:cd03238   132 IKGLIDL-GNTVILIEHN-LDVLSSADWIIDFGP 163
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 24-225 3.91e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 57.72  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  24 SFTVKKNEFVCLLGPSGCGKTTLLRILAG-----------------------LEEATTGSIAVNGKDItaLPPGKRNFGm 80
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqfshitrlsfeqLQKLVSDEWQRNNTDM--LSPGEDDTG- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  81 vfqsyalfpnLTALENIEYGLKakkygKAEVKEKALSALELVDLLNVKDKYpaqMSGGQQQRVALARALALSPDILLLDE 160
Cdd:PRK10938  100 ----------RTTAEIIQDEVK-----DPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 161 PLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEIMQIGTPEEIYQR 225
Cdd:PRK10938  162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 5-206 3.98e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.59  E-value: 3.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   5 LSIQHIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI--AVNGkditalppgkrNFGMVF 82
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENA-----------NIGYYA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  83 Q-SYALFPN-LTALENIeyglkaKKYGKAEVKEKALSALeLVDLLNVKD---KYPAQMSGGQQQRVALARALALSPDILL 157
Cdd:PRK15064  389 QdHAYDFENdLTLFDWM------SQWRQEGDDEQAVRGT-LGRLLFSQDdikKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1003869982 158 LDEPLSALDAKVREKLRREMrdlqEKVGVTTIMVTHDQEEALTMADKIV 206
Cdd:PRK15064  462 MDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRII 506
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 132-206 1.16e-08

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: 54.54  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 132 PAQMSGGQQQ------RVALARALALSPDILLLDEPLSALDA-KVREKLRREMRDLQEKVGVTTIMVTHDqEEALTMADK 204
Cdd:cd03240   113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADH 191


                  ..
gi 1003869982 205 IV 206
Cdd:cd03240   192 IY 193
PLN03073 PLN03073
ABC transporter F family; Provisional
 21-195 1.46e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.02  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  21 KDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI--------------AVNGKDITALPpgkrnfgMVFQSYA 86
Cdd:PLN03073  526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNP-------LLYMMRC 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  87 lFPnltalenieyglkakkyGKAEVKEKA-LSALELVDLLNVKDKYpaQMSGGQQQRVALARALALSPDILLLDEPLSAL 165
Cdd:PLN03073  599 -FP-----------------GVPEQKLRAhLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658

                         170       180       190
                  ....*....|....*....|....*....|
gi 1003869982 166 DAKVREKLRREMRDLQEKVgvttIMVTHDQ 195
Cdd:PLN03073  659 DLDAVEALIQGLVLFQGGV----LMVSHDE 684
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 20-208 1.55e-08

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 54.19  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTL----------LRILAGLEEATTGSIAVNGKD----ITALPP--------GKRN 77
Cdd:cd03270    11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMDKPdvdsIEGLSPaiaidqktTSRN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  78 ----FGMVFQSYALFPNLTALENIEYGLKAkkygkaeVKEKALSALELvdllnvkDKYPAQMSGGQQQRVALARAL--AL 151
Cdd:cd03270    91 prstVGTVTEIYDYLRLLFARVGIRERLGF-------LVDVGLGYLTL-------SRSAPTLSGGEAQRIRLATQIgsGL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 152 SPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDqEEALTMADKIVVM 208
Cdd:cd03270   157 TGVLYVLDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHD-EDTIRAADHVIDI 211
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 60-226 1.62e-08

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: 56.17  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  60 SIAVNGKDI---TALPpgkrnfgmVFQSYALFPNLTALENieyglkaKKYGKAEVKEKALSALE-LVDL----LNVkDKY 131
Cdd:TIGR00630 422 AVTVGGKSIadvSELS--------IREAHEFFNQLTLTPE-------EKKIAEEVLKEIRERLGfLIDVgldyLSL-SRA 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 132 PAQMSGGQQQRVALARAL--ALSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDqEEALTMADKIVVM- 208
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHD-EDTIRAADYVIDIg 563

                         170       180
                  ....*....|....*....|...
gi 1003869982 209 ----NH-AEIMQIGTPEEIYQRP 226
Cdd:TIGR00630 564 pgagEHgGEVVASGTPEEILANP 586
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 20-206 2.39e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.09  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNG--------KDITALP--------PGKRNFGMVFQ 83
Cdd:PRK10636   17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPqpaleyviDGDREYRQLEA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  84 SYAlfpnlTALENIEYGLKAKKYGKAE------VKEKALSALELVDLLNVKDKYPAQ-MSGGQQQRVALARALALSPDIL 156
Cdd:PRK10636   97 QLH-----DANERNDGHAIATIHGKLDaidawtIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003869982 157 LLDEPLSALDAKVREKLRREMRDLQEkvgvTTIMVTHDQEEALTMADKIV 206
Cdd:PRK10636  172 LLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII 217
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 134-208 4.81e-07

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: 48.90  E-value: 4.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003869982 134 QMSGGQQQRVALARALALS---PDIL-LLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDQEEALtMADKIVVM 208
Cdd:cd03227    77 QLSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAE-LADKLIHI 153
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 20-230 6.46e-07

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 49.91  E-value: 6.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGSIAVNGKDITALP--PGKRNFGMVFQSYALFPNltaleNI 97
Cdd:cd03288    37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG-----SI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  98 EYGLKAKKygkAEVKEKALSALELVDLLNVKDKYPAQM-----------SGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:cd03288   112 RFNLDPEC---KCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 167 AKVREKLRR-EMRDLQEKvgvTTIMVTHDQEEALTmADKIVVMNHAEIMQIGTPEEIYQRPANPF 230
Cdd:cd03288   189 MATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 133-221 1.79e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 49.83  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  133 AQMSGGQQQRVALARALA--LSPDILLLDEPLSALDAKVREKLRREMRDLQEKvGVTTIMVTHDqEEALTMADKIVVMN- 209
Cdd:PRK00635   475 ATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-EQMISLADRIIDIGp 552

                           90
                   ....*....|....*..
gi 1003869982  210 -----HAEIMQIGTPEE 221
Cdd:PRK00635   553 gagifGGEVLFNGSPRE 569
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 20-198 2.70e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.86  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLE-EATTGSIAVNGK---------DItalppgKRNFGMVFQSYAL-- 87
Cdd:PRK10938  276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLFGRrrgsgetiwDI------KKHIGYVSSSLHLdy 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNLTALENI------EYGLkakkYGKAEVKEKALsALELVDLLNVKD---KYPAQ-MSGGQQQRVALARALALSPDILL 157
Cdd:PRK10938  350 RVSTSVRNVIlsgffdSIGI----YQAVSDRQQKL-AQQWLDILGIDKrtaDAPFHsLSWGQQRLALIVRALVKHPTLLI 424

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1003869982 158 LDEPLSALDAKVREKLRREMRDLQEKVGVTTIMVTHDQEEA 198
Cdd:PRK10938  425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
PLN03073 PLN03073
ABC transporter F family; Provisional
 134-166 5.28e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.93  E-value: 5.28e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1003869982 134 QMSGGQQQRVALARALALSPDILLLDEPLSALD 166
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 35-166 7.96e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.19  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  35 LLGPSGCGKTTLLRILAGLEEATTGSIAvngkditaLPPGKRnFGMVFQSYALFPNLTALENIEYG----LKAKK----- 105
Cdd:PRK15064   32 LIGANGCGKSTFMKILGGDLEPSAGNVS--------LDPNER-LGKLRQDQFAFEEFTVLDTVIMGhtelWEVKQerdri 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 106 YGKAEVKEK-ALSALELVDLLNVKDKYPAQ--------------------MSG---GQQQRVALARALALSPDILLLDEP 161
Cdd:PRK15064  103 YALPEMSEEdGMKVADLEVKFAEMDGYTAEaragelllgvgipeeqhyglMSEvapGWKLRVLLAQALFSNPDILLLDEP 182


                  ....*
gi 1003869982 162 LSALD 166
Cdd:PRK15064  183 TNNLD 187
PLN03140 PLN03140
ABC transporter G family member; Provisional
 18-247 1.60e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 46.76  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   18 TALKDISFTVKKNEFVCLLGPSGCGKTTLLRILAG-LEEA--TTGSIAVNGKDITALPPGKRNfGMVFQSYALFPNLTAL 94
Cdd:PLN03140   179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlkVSGEITYNGYRLNEFVPRKTS-AYISQNDVHVGVMTVK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982   95 ENIEYGLKAKKYG--------------------KAEVK--EKAlSALELVD----------LLN--------VKDKYPAQ 134
Cdd:PLN03140   258 ETLDFSARCQGVGtrydllselarrekdagifpEAEVDlfMKA-TAMEGVKsslitdytlkILGldickdtiVGDEMIRG 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  135 MSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLrreMRDLQEKVGVT--TIMVTHDQ--EEALTMADKIVVMNH 210
Cdd:PLN03140   337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI---VKCLQQIVHLTeaTVLMSLLQpaPETFDLFDDIILLSE 413

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1003869982  211 AEIMQIGTPEEI--------YQRPANPFVADFIGSINffSKNNEE 247
Cdd:PLN03140   414 GQIVYQGPRDHIleffescgFKCPERKGTADFLQEVT--SKKDQE 456
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 249-324 2.77e-05

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: 41.45  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1003869982 249 AIRPEHVTVV-QNNGMKTIVESMEFRGSVYRTEVRVIDekthlynEKIVVDILASEVEkTAIRKGQPIQISFSENHM 324
Cdd:pfam08402   2 AIRPEKIRLAaAANGLSGTVTDVEYLGDHTRYHVELAG-------GEELVVRVPNAHA-RPPAPGDRVGLGWDPEDA 70
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-213 3.09e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.55  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEAT--TGSIAVNGKDIT------ALPPG----------------- 74
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDvstvsdAIDAGlayvtedrkgyglnlid 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  75 --KRNFGMvfqsyalfPNLTAL-------ENIEYGLkAKKYgKAEVKEKALSALELVdllnvkdkypAQMSGGQQQRVAL 145
Cdd:NF040905  356 diKRNITL--------ANLGKVsrrgvidENEEIKV-AEEY-RKKMNIKTPSVFQKV----------GNLSGGNQQKVVL 415

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003869982 146 ARALALSPDILLLDEPLSALD--AKVreklrrE----MRDLQEKvGVTTIMVTHDQEEALTMADKIVVMNHAEI 213
Cdd:NF040905  416 SKWLFTDPDVLILDEPTRGIDvgAKY------EiytiINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 12-208 2.15e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.87  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  12 KQFDAFTALKDISFT-VKKNEFVCLLGPSGCGKTTLLrilagleEATTgsIAVNGKditalPPGKRNFG---MVFQSYAL 87
Cdd:cd03279     9 KNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTIL-------DAIT--YALYGK-----TPRYGRQEnlrSVFAPGED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  88 FPNLT---ALENIEYglKAKKYGKAEVKEKALSAL----ELVDLL--NVKdkypaQMSGGQQQRVALARALALSP----- 153
Cdd:cd03279    75 TAEVSftfQLGGKKY--RVERSRGLDYDQFTRIVLlpqgEFDRFLarPVS-----TLSGGETFLASLSLALALSEvlqnr 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003869982 154 -----DILLLDEPLSALDAKVREKLR---REMRDLQEKVGVttimVTHDQEEALTMADKIVVM 208
Cdd:cd03279   148 ggarlEALFIDEGFGTLDPEALEAVAtalELIRTENRMVGV----ISHVEELKERIPQRLEVI 206
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 35-195 3.17e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 42.46  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  35 LLGPSGCGKTTLLRILAGLEEATTGSIAVnGKDItalppgKRNFGMVFQSYALFPNLTALENIeyglkakkygkAEVKEK 114
Cdd:PRK10636  343 LLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI------KLGYFAQHQLEFLRADESPLQHL-----------ARLAPQ 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 115 ALSAlELVDLL--------NVKDKyPAQMSGGQQQRVALARALALSPDILLLDEPLSALDAKVREKLRREMRDLQEKVgv 186
Cdd:PRK10636  405 ELEQ-KLRDYLggfgfqgdKVTEE-TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL-- 480


                  ....*....
gi 1003869982 187 ttIMVTHDQ 195
Cdd:PRK10636  481 --VVVSHDR 487
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
12-194 4.45e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 40.76  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  12 KQFDAFTALKDISFTvkkNEFVCLLGPSGCGKTTLLR-ILAGLEEATTGS--------------------IAVNGKDITA 70
Cdd:COG0419     8 ENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEaIRYALYGKARSRsklrsdlinvgseeasveleFEHGGKRYRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  71 LPP-GKRNFGMVFQSYALFPNLTALENIEYGLKAKKYGKaEVKEKALSAL-ELVDLLNVKDKY---------PAQMSGGQ 139
Cdd:COG0419    85 ERRqGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLK-ELEEALESALeELAELQKLKQEIlaqlsgldpIETLSGGE 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003869982 140 QQRVALARALAlspdiLLLDepLSALDAKVREKLRREMRDLQekvgvttiMVTHD 194
Cdd:COG0419   164 RLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
recF PRK00064
recombination protein F; Reviewed
 136-213 9.60e-04

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 40.53  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 136 SGGQQqrvalaRALALS----------------PdILLLDEPLSALDAKVREKLRREMRDLQEKVGVTTImvTHDQEEAL 199
Cdd:PRK00064  275 STGQQ------KLLLLAlklaeaellkeetgeaP-ILLLDDVASELDDGRRAALLERLKGLGAQVFITTT--DLEDLADL 345

                          90
                  ....*....|....
gi 1003869982 200 TMADKIVVMNHAEI 213
Cdd:PRK00064  346 LENAKIFHVEQGKI 359
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
136-227 1.34e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 40.39  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 136 SGGQQQRVALARAL--ALSpDIL-LLDEP---LSALD-AKVREKLRReMRDLqekvGVTTIMVTHDqEEALTMADKIVVM 208
Cdd:COG0178   487 SGGEAQRIRLATQIgsGLV-GVLyVLDEPsigLHQRDnDRLIETLKR-LRDL----GNTVIVVEHD-EDTIRAADYIIDI 559

                          90       100
                  ....*....|....*....|....*
gi 1003869982 209 -----NH-AEIMQIGTPEEIYQRPA 227
Cdd:COG0178   560 gpgagEHgGEVVAQGTPEEILKNPD 584
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 29-61 1.69e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.92  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1003869982  29 KNEFVCLLGPSGCGKTTLLRILAGLEEATTGSI 61
Cdd:cd01854    84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 9-51 1.87e-03

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 39.94  E-value: 1.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1003869982   9 HIQKQFDAFTALKDISFTVKKNEFVCLLGPSGCGKTTLLRILA 51
Cdd:TIGR00602  89 HKKKIEEVETWLKAQVLENAPKRILLITGPSGCGKSTTIKILS 131
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 133-179 2.01e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 36.83  E-value: 2.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 133 AQMSGGQQQR-VALARALALS------------PDILLLDEPLSALDAKVREKLRREMRD 179
Cdd:pfam13558  31 GGLSGGEKQLlAYLPLAAALAaqygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
AAA_28 pfam13521
AAA domain;
32-51 2.60e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 38.01  E-value: 2.60e-03
                          10        20
                  ....*....|....*....|
gi 1003869982  32 FVCLLGPSGCGKTTLLRILA 51
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALA 20
PRK15177 PRK15177
Vi polysaccharide ABC transporter ATP-binding protein VexC;
20-106 6.08e-03

Vi polysaccharide ABC transporter ATP-binding protein VexC;


Pssm-ID: 185099 [Multi-domain]  Cd Length: 213  Bit Score: 37.35  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982  20 LKDISFTVKKNEFVCLLGPSGCGKTTLLRILAGLEEATTGS-IAVNGKditALPPGKRNFgmvfqsyaLFPNLTALENIE 98
Cdd:PRK15177    3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGD---ALPLGANSF--------ILPGLTGEENAR 71

                          90
                  ....*....|...
gi 1003869982  99 -----YGLKAKKY 106
Cdd:PRK15177   72 mmaslYGLDGDEF 84
uvrA PRK00349
excinuclease ABC subunit UvrA;
136-222 8.26e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.13  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003869982 136 SGGQQQRVALARAL--ALSPDILLLDEPLSALDAKVREKL---RREMRDLqekvGVTTIMVTHDqEEALTMADKIVVM-- 208
Cdd:PRK00349  491 SGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNDRLietLKHLRDL----GNTLIVVEHD-EDTIRAADYIVDIgp 565

                          90
                  ....*....|....*...
gi 1003869982 209 ---NH-AEIMQIGTPEEI 222
Cdd:PRK00349  566 gagVHgGEVVASGTPEEI 583
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 33-53 8.86e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 36.12  E-value: 8.86e-03
                          10        20
                  ....*....|....*....|.
gi 1003869982  33 VCLLGPSGCGKTTLLRILAGL 53
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAA 22
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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