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Conserved domains on  [gi|2674892663|ref|WP_331870448|]
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ATP-binding cassette domain-containing protein [Megamonas funiformis]

Protein Classification

amino acid ABC transporter ATP-binding/permease protein( domain architecture ID 11471986)

amino acid ABC transporter ATP-binding/permease protein similar to the CydC and CydD subunits of thiol reductant ABC transporter, which exports glutathione and cysteine to the periplasm; both subunits contain an N-terminal membrane-spanning domain and a C-terminal ATP-binding domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
8-559 8.93e-137

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: 409.16  E-value: 8.93e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG4987     9 LLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  88 SFRVFVLIKIIKALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIF 166
Cdd:COG4987    89 DLRVRLYRRLEPLAPAGlARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPYMIWRRYLKLKKHKFLLTQEI----IEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEF 242
Cdd:COG4987   169 GLLLPLLAARLGRRAGRRLAAARAALrarlTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 243 IMGAYLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDlaifmqekkfIANTNNE 319
Cdd:COG4987   249 AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRvraAARRLNE----------LLDAPPA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG4987   319 VTEPAEPAPAPGGPSLELEDVSFRYPgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG4987   399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALpdGLDTWLGEGGRRLSGGERR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG4987   479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558

                  ....*
gi 2674892663 555 REDSY 559
Cdd:COG4987   559 QNGRY 563
 
Name Accession Description Interval E-value
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
8-559 8.93e-137

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: 409.16  E-value: 8.93e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG4987     9 LLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  88 SFRVFVLIKIIKALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIF 166
Cdd:COG4987    89 DLRVRLYRRLEPLAPAGlARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPYMIWRRYLKLKKHKFLLTQEI----IEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEF 242
Cdd:COG4987   169 GLLLPLLAARLGRRAGRRLAAARAALrarlTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 243 IMGAYLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDlaifmqekkfIANTNNE 319
Cdd:COG4987   249 AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRvraAARRLNE----------LLDAPPA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG4987   319 VTEPAEPAPAPGGPSLELEDVSFRYPgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG4987   399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALpdGLDTWLGEGGRRLSGGERR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG4987   479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558

                  ....*
gi 2674892663 555 REDSY 559
Cdd:COG4987   559 QNGRY 563
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
9-525 8.85e-74

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: 244.58  E-value: 8.85e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   9 IRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTS 88
Cdd:TIGR02868   8 LKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  89 FRVFVLIKIIK-ALPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIIT--TISVFILSIWFFlySYDLMILLISSWLI 165
Cdd:TIGR02868  88 LRVRVYERLARqALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAlvVGAAAVAAIAVL--SVPAALILAAGLLL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 166 FMIVIPYMIWR----RYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSE 241
Cdd:TIGR02868 166 AGFVAPLVSLRaaraAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 242 FIMGA--YLVICLAISIYLVNTQDfnPIMAITIILTYQAVLEVLAMMPSLIEHFdeasKRWQDLAIFMQEKKFIANTNNE 319
Cdd:TIGR02868 246 LAAGLavLGALWAGGPAVADGRLA--PVTLAVLVLLPLAAFEAFAALPAAAQQL----TRVRAAAERIVEVLDAAGPVAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNY 397
Cdd:TIGR02868 320 GSAPAAGAVGLGKPTLELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 DDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHR 475
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQR 479
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 476 LQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHD 525
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
14-559 1.73e-62

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 215.46  E-value: 1.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  14 WSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLS----LAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSF 89
Cdd:PRK11160   16 FMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSfnymLPAAGVRGAAIGRTAGRYGERLVSHDATFRVLTHL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  90 RVFVLIKIIKALPFKQQT-ENGDAFDLIVNAVDNLRDSFLRFfLPPIITTISVfILSIWFFLYSYD--LMILLISSWLIF 166
Cdd:PRK11160   96 RVFTFSKLLPLSPAGLARyRQGDLLNRLVADVDTLDHLYLRL-ISPLVAALVV-ILVLTIGLSFFDltLALTLGGILLLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPymiWRRYLKLKKHKFLLTQE-------IIEFYEGNRELSFYNY-DKYRlKNINHSIEQYQQYQQNLFKLKLKVNL 238
Cdd:PRK11160  174 LLLLP---LLFYRLGKKPGQDLTHLraqyrvqLTEWLQGQAELTLFGAeDRYR-QQLEQTEQQWLAAQRRQANLTGLSQA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 239 CSEFIMGAYLVICLAISIYLVNTQDF-NPIMAItIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDLaifMQEKKfia 314
Cdd:PRK11160  250 LMILANGLTVVLMLWLAAGGVGGNAQpGALIAL-FVFAALAAFEALMPVAGAFQHLGQviaSARRINEI---TEQKP--- 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 315 ntnnEIKSENQEDKQSKDVQLLLKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIF 391
Cdd:PRK11160  323 ----EVTFPTTSTAAADQVSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 392 IQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENV---YLLDfvNQVGLDYIVGNDGNKL 468
Cdd:PRK11160  399 LNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVgleKLLE--DDKGLNAWLGEGGRQL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK11160  477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
                         570
                  ....*....|.
gi 2674892663 549 IKKLLLREDSY 559
Cdd:PRK11160  557 HQELLAQQGRY 567
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
338-555 2.24e-49

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: 170.48  E-value: 2.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:cd03254     6 ENVNFSYDekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03254    86 TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 494 PTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03254   166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
349-496 1.38e-34

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: 127.76  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFN-LSIRDN- 426
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENl 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 427 -----FKMLYENITDEEIYKSLENVYLLDFVNQVgldyiVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:pfam00005  81 rlgllLKGLSKREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
343-538 1.01e-15

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 75.73  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaekSIREHFAVAFQEHHI--- 418
Cdd:NF040873    1 GYGgRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVPQRSevp 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 --FNLSIRDNFKM-------LYENITDE---EIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQ 485
Cdd:NF040873   68 dsLPLTVRDLVAMgrwarrgLWRRLTRDdraAVDDALERVGLADLAGrQLG----------ELSGGQRQRALLAQGLAQE 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLM--EKYQKQTMIVTSHDISLLRFFDDIIIC 538
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERI-IALLaeEHARGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
358-537 1.47e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.06  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  358 KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIqgknyddlaeksirehfavafqehhifnlsirdnfkmlyenITDE 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  438 EIYKSLENVYLLDfvnqvgldyIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL------- 510
Cdd:smart00382  40 DILEEVLDQLLLI---------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllll 110
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2674892663  511 MEKYQKQTMIVTSHDIS------LLRFFDDIII 537
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpalLRRRFDRRIV 143
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
450-552 1.93e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 43.96  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 450 DFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDIS 527
Cdd:NF000106  127 ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrsMVRDGATVLLTTQYMEE 206
                          90       100
                  ....*....|....*....|....*
gi 2674892663 528 LLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:NF000106  207 AEQLAHELTVIDRGRVIADGKVDEL 231
 
Name Accession Description Interval E-value
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
8-559 8.93e-137

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: 409.16  E-value: 8.93e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG4987     9 LLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  88 SFRVFVLIKIIKALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIF 166
Cdd:COG4987    89 DLRVRLYRRLEPLAPAGlARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPYMIWRRYLKLKKHKFLLTQEI----IEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEF 242
Cdd:COG4987   169 GLLLPLLAARLGRRAGRRLAAARAALrarlTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 243 IMGAYLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDlaifmqekkfIANTNNE 319
Cdd:COG4987   249 AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRvraAARRLNE----------LLDAPPA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG4987   319 VTEPAEPAPAPGGPSLELEDVSFRYPgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG4987   399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALpdGLDTWLGEGGRRLSGGERR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG4987   479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558

                  ....*
gi 2674892663 555 REDSY 559
Cdd:COG4987   559 QNGRY 563
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
9-525 8.85e-74

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: 244.58  E-value: 8.85e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   9 IRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTS 88
Cdd:TIGR02868   8 LKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  89 FRVFVLIKIIK-ALPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIIT--TISVFILSIWFFlySYDLMILLISSWLI 165
Cdd:TIGR02868  88 LRVRVYERLARqALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAlvVGAAAVAAIAVL--SVPAALILAAGLLL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 166 FMIVIPYMIWR----RYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSE 241
Cdd:TIGR02868 166 AGFVAPLVSLRaaraAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 242 FIMGA--YLVICLAISIYLVNTQDfnPIMAITIILTYQAVLEVLAMMPSLIEHFdeasKRWQDLAIFMQEKKFIANTNNE 319
Cdd:TIGR02868 246 LAAGLavLGALWAGGPAVADGRLA--PVTLAVLVLLPLAAFEAFAALPAAAQQL----TRVRAAAERIVEVLDAAGPVAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNY 397
Cdd:TIGR02868 320 GSAPAAGAVGLGKPTLELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 DDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHR 475
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQR 479
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 476 LQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHD 525
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
8-559 3.99e-68

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 230.82  E-value: 3.99e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG1132    15 YLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  88 SFRVFVLIKIIKaLPFKQQTEN--GDAFDLIVNAVDNLRDsFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLI 165
Cdd:COG1132    95 DLRRDLFEHLLR-LPLSFFDRRrtGDLLSRLTNDVDAVEQ-FLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 166 FMIVIPY----MIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSE 241
Cdd:COG1132   173 LLLLVLRlfgrRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLME 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 242 FIMGAYLVICLAISIYLVNTQDFNP---IMAITIILTYQAVLEVLAMMPSLIEhfdEASKRWQDLAIFMQEKKFIANTNN 318
Cdd:COG1132   253 LLGNLGLALVLLVGGLLVLSGSLTVgdlVAFILYLLRLFGPLRQLANVLNQLQ---RALASAERIFELLDEPPEIPDPPG 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 319 EIKSENQEDkqskDVQLllKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG1132   330 AVPLPPVRG----EIEF--ENVSFSYpgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG1132   404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQ 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG1132   484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563

                  ....*
gi 2674892663 555 REDSY 559
Cdd:COG1132   564 RGGLY 568
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
5-559 4.38e-67

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: 230.88  E-value: 4.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   5 LSNMIRPVVWSLLLAILVGTISTLSSISLMGLSAWLI---ASAALQPPLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKV 81
Cdd:COG2274   147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIdrvLPNQDLSTLWVLAIGLLLA---LLFEGLLRLLRSYLLLRL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  82 GFSLFTSFRVFVLIKIIKaLPFKQqTENGDAFDLI--VNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILL 159
Cdd:COG2274   224 GQRIDLRLSSRFFRHLLR-LPLSF-FESRSVGDLAsrFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 160 ISSWLIFMIVIPYMIWRRYLKLKKHKFLLTQE---IIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKV 236
Cdd:COG2274   302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRqslLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 237 NLCSEFIMGAYLVICLAISIYLVNTQDFNP--IMAITIILTYqavleVLAMMPSLIEHFDeaskRWQDLAIFMQEKKFIA 314
Cdd:COG2274   382 STLSGLLQQLATVALLWLGAYLVIDGQLTLgqLIAFNILSGR-----FLAPVAQLIGLLQ----RFQDAKIALERLDDIL 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 315 NTnneiKSENQEDKQSKDVQLL-----LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPL 386
Cdd:COG2274   453 DL----PPEREEGRSKLSLPRLkgdieLENVSFRYPgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 387 KGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGND 464
Cdd:COG2274   529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALpmGYDTVVGEG 608
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 465 GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKII 544
Cdd:COG2274   609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
                         570
                  ....*....|....*
gi 2674892663 545 EQGNIKKLLLREDSY 559
Cdd:COG2274   689 EDGTHEELLARKGLY 703
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
5-553 3.31e-64

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: 220.01  E-value: 3.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   5 LSNMIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAAL-QPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGF 83
Cdd:COG4988     8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIgGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  84 SLFTSFRVFVLIKIIKALP-FKQQTENGDAFDLIVNAVDNLrDSFLRFFLPPIITTISVFILsIWFFLYSYDL---MILL 159
Cdd:COG4988    88 RVKRRLRRRLLEKLLALGPaWLRGKSTGELATLLTEGVEAL-DGYFARYLPQLFLAALVPLL-ILVAVFPLDWlsgLILL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 160 ISSWLI--FMIVIPYMiwrrylklkkhkfllTQEIIE------------FYE---GNRELSFYNYDKYRLKNINHSIEQY 222
Cdd:COG4988   166 VTAPLIplFMILVGKG---------------AAKASRrqwralarlsghFLDrlrGLTTLKLFGRAKAEAERIAEASEDF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 223 QQyqqnlfklK----LKVNLCSEFIM--GAYLVICLA---ISIYLVNTQdfnpimaitiiLTYQAVLEVLAMMPSLIEHF 293
Cdd:COG4988   231 RK--------RtmkvLRVAFLSSAVLefFASLSIALVavyIGFRLLGGS-----------LTLFAALFVLLLAPEFFLPL 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 294 DEASKRWQDLA--------IFmqekKFIANTNNEIKSENQEDKQSKDVQLLLKDLAYGYD--KVLLKDINLSIKKGNKTL 363
Cdd:COG4988   292 RDLGSFYHARAngiaaaekIF----ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPggRPALDGLSLTIPPGERVA 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSL 443
Cdd:COG4988   368 LVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAAL 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 444 ENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIV 521
Cdd:COG4988   448 EAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
                         570       580       590
                  ....*....|....*....|....*....|..
gi 2674892663 522 TSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4988   528 ITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
14-559 1.73e-62

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 215.46  E-value: 1.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  14 WSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLS----LAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSF 89
Cdd:PRK11160   16 FMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSfnymLPAAGVRGAAIGRTAGRYGERLVSHDATFRVLTHL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  90 RVFVLIKIIKALPFKQQT-ENGDAFDLIVNAVDNLRDSFLRFfLPPIITTISVfILSIWFFLYSYD--LMILLISSWLIF 166
Cdd:PRK11160   96 RVFTFSKLLPLSPAGLARyRQGDLLNRLVADVDTLDHLYLRL-ISPLVAALVV-ILVLTIGLSFFDltLALTLGGILLLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPymiWRRYLKLKKHKFLLTQE-------IIEFYEGNRELSFYNY-DKYRlKNINHSIEQYQQYQQNLFKLKLKVNL 238
Cdd:PRK11160  174 LLLLP---LLFYRLGKKPGQDLTHLraqyrvqLTEWLQGQAELTLFGAeDRYR-QQLEQTEQQWLAAQRRQANLTGLSQA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 239 CSEFIMGAYLVICLAISIYLVNTQDF-NPIMAItIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDLaifMQEKKfia 314
Cdd:PRK11160  250 LMILANGLTVVLMLWLAAGGVGGNAQpGALIAL-FVFAALAAFEALMPVAGAFQHLGQviaSARRINEI---TEQKP--- 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 315 ntnnEIKSENQEDKQSKDVQLLLKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIF 391
Cdd:PRK11160  323 ----EVTFPTTSTAAADQVSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 392 IQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENV---YLLDfvNQVGLDYIVGNDGNKL 468
Cdd:PRK11160  399 LNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVgleKLLE--DDKGLNAWLGEGGRQL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK11160  477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
                         570
                  ....*....|.
gi 2674892663 549 IKKLLLREDSY 559
Cdd:PRK11160  557 HQELLAQQGRY 567
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
338-555 2.24e-49

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: 170.48  E-value: 2.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:cd03254     6 ENVNFSYDekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03254    86 TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 494 PTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03254   166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
337-537 3.35e-45

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: 158.78  E-value: 3.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03225     2 LKNLSFSYPdgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRD--NFKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:cd03225    82 QnpDDQFFGPTVEEevAFGLENLGLPEEEIEERVEEA-----LELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 490 LLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLR-FFDDIII 537
Cdd:cd03225   157 LLDEPTAGLDPAGRREL-LELLKKLKAEgkTIIIVTHDLDLLLeLADRVIV 206
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
337-537 5.19e-45

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 156.77  E-value: 5.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03228     3 FKNVSFSYPgrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03228    83 QDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674892663 494 PTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:cd03228   123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIV 166
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
337-559 1.07e-42

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: 152.77  E-value: 1.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:cd03253     3 FENVTFAYDpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:cd03253    83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 493 EPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03253   163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
337-559 4.21e-41

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 148.53  E-value: 4.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03251     3 FKNVTFRYPGdgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03251    83 QDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03251   163 DEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
337-557 7.94e-41

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: 147.48  E-value: 7.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:COG1122     3 LENLSFSYpgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 --EHHIFNLSIRD-------NFKMLYENItDEEIYKSLENVYLLDFvnqvgLDYIVgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:COG1122    83 npDDQLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHL-----ADRPP----HELSGGQKQRVAIAGVLAME 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:COG1122   153 PEVLVLDEPTAGLDPRGRREL-LELLKRLNKEgkTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
9-559 1.34e-40

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: 155.26  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   9 IRPVVWSLLLAIL-----VGTISTLSSIS---LMGLSAWLIASAALQPPLYVLSLAIVgvrfcgvmRAVFRYLERYFTHK 80
Cdd:TIGR02203   9 VRPYKAGLVLAGVamilvAATESTLAALLkplLDDGFGGRDRSVLWWVPLVVIGLAVL--------RGICSFVSTYLLSW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  81 VGFSLFTSFRVFVLIKIIKaLP--FKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMil 158
Cdd:TIGR02203  81 VSNKVVRDIRVRMFEKLLG-LPvsFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 159 lisswLIFMIVIPYMIW--RRYLKLKKHKFLLTQEII--------EFYEGNRELSFYNYDKYRLKninhsieQYQQYQQN 228
Cdd:TIGR02203 158 -----LIVVVMLPVLSIlmRRVSKRLRRISKEIQNSMgqvttvaeETLQGYRVVKLFGGQAYETR-------RFDAVSNR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 229 LFKLKLKV----NLCSEFIMgayLVICLAISIylvntqdfnpIMAITIILT---YQAVLEVLAMMPSLIEHFDeASKRWQ 301
Cdd:TIGR02203 226 NRRLAMKMtsagSISSPITQ---LIASLALAV----------VLFIALFQAqagSLTAGDFTAFITAMIALIR-PLKSLT 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 302 DLAIFMQEKKFIANTNNEIKSENQE-DKQSKDVQLLLKDLAY--------GYDKVLLKDINLSIKKGNKTLIVGTSGCGK 372
Cdd:TIGR02203 292 NVNAPMQRGLAAAESLFTLLDSPPEkDTGTRAIERARGDVEFrnvtfrypGRDRPALDSISLVIEPGETVALVGRSGSGK 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 373 STLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKmlY---ENITDEEIYKSLENVYLL 449
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA--YgrtEQADRAEIERALAAAYAQ 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 450 DFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS 527
Cdd:TIGR02203 450 DFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLS 529
                         570       580       590
                  ....*....|....*....|....*....|..
gi 2674892663 528 LLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR02203 530 TIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
ABC_6TM_CydC cd18585
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...
23-299 7.57e-40

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350029 [Multi-domain]  Cd Length: 290  Bit Score: 146.86  E-value: 7.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  23 GTISTLSSISLMGLSAWLIASAALQP---PLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVLIKIIK 99
Cdd:cd18585     1 GLLTLLASIGLLALSGWFISAAALAGlaaPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 100 ALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPYMIWRRY 178
Cdd:cd18585    81 LAPARlQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 179 LKLKKHKFLLT----QEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVICLAI 254
Cdd:cd18585   161 KKIGQQLVQLRaelrTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2674892663 255 SIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKR 299
Cdd:cd18585   241 GAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGEtraAARR 288
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
16-536 8.95e-40

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: 152.06  E-value: 8.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  16 LLLAILVGTISTLSSISLMGLSAWLIASAALQ-PPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVL 94
Cdd:TIGR02857   5 LALLALLGVLGALLIIAQAWLLARVVDGLISAgEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  95 IKIIKALPFKQQTEN-GDAFDLIVNAVDNLRDSFLRFfLPPII--TTISVFILSIWFFLYSYDLMILLISSWLI--FMIV 169
Cdd:TIGR02857  85 EAVAALGPRWLQGRPsGELATLALEGVEALDGYFARY-LPQLVlaVIVPLAILAAVFPQDWISGLILLLTAPLIpiFMIL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 170 IPYMIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKlkvnlcseFIMGAYLV 249
Cdd:TIGR02857 164 IGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIA--------FLSSAVLE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 250 ICLAISIYLVntqdfnpimAITI-------ILTYQAVLEVLAMMPSLIEHFDEASKRWQDLAIFMQEKKFIANT--NNEI 320
Cdd:TIGR02857 236 LFATLSVALV---------AVYIgfrllagDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVldAAPR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKD-VQLLLKDL--AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNY 397
Cdd:TIGR02857 307 PLAGKAPVTAAPaSSLEFSGVsvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 DDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHR 475
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQR 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 476 LQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDII 536
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
310-548 1.91e-38

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 149.22  E-value: 1.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 310 KKFIANTNNEIKSENQEDKQSKDVQLLLKDLA-YGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLK 387
Cdd:PRK11174  325 VTFLETPLAHPQQGEKELASNDPVTIEAEDLEiLSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQ 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 388 GNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDG 465
Cdd:PRK11174  404 GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQA 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 466 NKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIE 545
Cdd:PRK11174  484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563

                  ...
gi 2674892663 546 QGN 548
Cdd:PRK11174  564 QGD 566
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
337-547 4.79e-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: 139.65  E-value: 4.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03245     5 FRNVSFSYPnqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ--VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03245    85 QDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03245   165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
337-564 9.94e-37

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: 136.65  E-value: 9.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVA 412
Cdd:COG1127     8 VRNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIGML 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN--FKML-YENITDEEIYKSLENVylldfVNQVGLDyivgNDGNK----LSGGQKHRLQLAICLAK 484
Cdd:COG1127    88 FQGGALFdSLTVFENvaFPLReHTDLSEAEIRELVLEK-----LELVGLP----GAADKmpseLSGGMRKRVALARALAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYL 560
Cdd:COG1127   159 DPEILLYDEPTAGLDPITSAVI-DELIRELRDElglTSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEELLASDDPWV 237

                  ....
gi 2674892663 561 NKLI 564
Cdd:COG1127   238 RQFL 241
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
337-556 1.74e-36

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: 136.33  E-value: 1.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:COG1120     4 AENLSVGYGgRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI-FNLSIRD-----------NFKMLYEniTDEEI-YKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICL 482
Cdd:COG1120    84 PPApFGLTVRElvalgryphlgLFGRPSA--EDREAvEEALE---------RTGLEHLADRPVDELSGGERQRVLIARAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 483 AKQKDIILLDEPTAGLDIKttNNIcsQLME------KYQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:COG1120   153 AQEPPLLLLDEPTSHLDLA--HQL--EVLEllrrlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228

                  .
gi 2674892663 556 E 556
Cdd:COG1120   229 E 229
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
335-549 2.52e-36

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 134.56  E-value: 2.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:COG4619     1 LELEGLSFRVGgKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLY----ENITDEEIYKSLEnvylldfvnQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG4619    81 QEPALWGGTVRDNLPFPFqlreRKFDRERALELLE---------RLGLPpDILDKPVERLSGGERQRLALIRALLLQPDV 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFFDDIIICgeekiIEQGNI 549
Cdd:COG4619   152 LLLDEPTSALDPENTRRVE-ELLREYLAEegrAVLWVSHDPEQIERVADRVLT-----LEAGRL 209
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
349-559 8.37e-36

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: 134.20  E-value: 8.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03249    19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:cd03249    99 YGKPDATDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 507 CSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03249   179 QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
337-552 1.33e-35

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: 133.07  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLY-----PLKGNIFIQGKNYDDLAEK--SIREH 408
Cdd:cd03260     3 LRDLNVYYgDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIFNLSIRDN-------FKMLYENITDEEIYKSLENVYLLDFVNQvgldyivGNDGNKLSGGQKHRLQLAIC 481
Cdd:cd03260    83 VGMVFQKPNPFPGSIYDNvayglrlHGIKLKEELDERVEEALRKAALWDEVKD-------RLHALGLSGGQQQRLCLARA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ-TMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:cd03260   156 LANEPEVLLLDEPTSALDPISTAKI-EELIAELKKEyTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
349-548 1.54e-35

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: 132.62  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNfk 428
Cdd:cd03244    20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSN-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 mL--YENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:cd03244    98 -LdpFGEYSDEELWQALERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674892663 505 NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:cd03244   177 LIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
337-561 6.66e-35

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: 131.47  E-value: 6.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVA 412
Cdd:cd03261     3 LRGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDN--FkMLYEN--ITDEEIYKSlenvyLLDFVNQVGLdyivGNDGNK----LSGGQKHRLQLAICLA 483
Cdd:cd03261    83 FQSGALFDsLTVFENvaF-PLREHtrLSEEEIREI-----VLEKLEAVGL----RGAEDLypaeLSGGMKKRVALARALA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03261   153 LDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKElglTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231

                  ..
gi 2674892663 560 LN 561
Cdd:cd03261   232 VR 233
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
337-547 1.24e-34

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: 128.71  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQe 415
Cdd:cd03214     2 VENLSVGYgGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeeiykSLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03214    81 --------------------------ALELLGLAHLADR---------PFNELSGGERQRVLLARALAQEPPILLLDEPT 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNICSQLME--KYQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:cd03214   126 SHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
339-555 1.28e-34

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 138.17  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEH 416
Cdd:PRK13657  339 DVSFSYDnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK13657  419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 495 TAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:PRK13657  499 TSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
349-496 1.38e-34

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: 127.76  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFN-LSIRDN- 426
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENl 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 427 -----FKMLYENITDEEIYKSLENVYLLDFVNQVgldyiVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:pfam00005  81 rlgllLKGLSKREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
342-561 1.29e-33

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 127.99  E-value: 1.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFN 420
Cdd:cd03252    10 YKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:cd03252    90 RSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 499 DIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLN 561
Cdd:cd03252   170 DYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
349-549 1.84e-33

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: 126.84  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHH-IFNLSI 423
Cdd:cd03255    20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNlLPDLTA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDN--FKMLYENITDEEIYKSLEnvYLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03255   100 LENveLPLLLAGVPKKERRERAE--ELLE---RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 502 TTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNI 549
Cdd:cd03255   175 TGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRII------ELRDGKI 218
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
335-547 7.73e-33

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: 123.96  E-value: 7.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaEKSIREHFAV 411
Cdd:cd03247     1 LSINNVSFSYpeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03247    80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03247   123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
349-536 1.06e-32

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 125.16  E-value: 1.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHHIF-NLSI 423
Cdd:COG1136    24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLpELTA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKM--LYENITDEEIYKSLEnvYLLDfvnQVGLDYIVGNDGNKLSGGQKHRlqLAIC--LAKQKDIILLDEPTAGLD 499
Cdd:COG1136   104 LENVALplLLAGVSRKERRERAR--ELLE---RVGLGDRLDHRPSQLSGGQQQR--VAIAraLVNRPKLILADEPTGNLD 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674892663 500 IKTTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:COG1136   177 SKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVI 215
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
337-536 1.25e-32

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: 124.57  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlaeksIREHFAVAFQE 415
Cdd:cd03235     2 VEDLTVSYGgHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI---FNLSIRD----------NFKMLYENITDEEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAIC 481
Cdd:cd03235    77 RSIdrdFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELADrQIG----------ELSGGQQQRVLLARA 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSqLMEKYQKQ--TMIVTSHDI-SLLRFFDDII 536
Cdd:cd03235   147 LVQDPDLLLLDEPFAGVDPKTQEDIYE-LLRELRREgmTILVVTHDLgLVLEYFDRVL 203
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
337-549 1.30e-32

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: 125.36  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQE 415
Cdd:COG4555     4 VENLSKKYGKVPaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNFKMLYE--NITDEEIYKSLEN-VYLLDFVNQvgLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG4555    83 RGLYdRLTVRENIRYFAElyGLFDEELKKRIEElIELLGLEEF--LDRRVG----ELSTGMKKKVALARALVHDPKVLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNI 549
Cdd:COG4555   157 DEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSL 216
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
343-559 1.61e-32

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 131.68  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PRK11176  353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDT 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENI-TDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK11176  433 IANNIAYARTEQySREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 500 IKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:PRK11176  513 TESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
337-536 2.60e-32

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 124.43  E-value: 2.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsirehfaVAF-- 413
Cdd:COG1121     9 LENLTVSYGgRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-------IGYvp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHI---FNLSIRDNFKM-LYENI--------TD-EEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLA 479
Cdd:COG1121    82 QRAEVdwdFPITVRDVVLMgRYGRRglfrrpsrADrEAVDEALERVGLEDLADrPIG----------ELSGGQQQRVLLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLR-FFDDII 536
Cdd:COG1121   152 RALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELRREgkTILVVTHDLGAVReYFDRVL 210
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
342-561 2.78e-32

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 124.02  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQEHHIF-N 420
Cdd:COG1131    10 YG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYpD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVNQ-VGldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG1131    88 LTVRENLRFfarLYglpRKEARERIDELLELFGLTDAADRkVG----------TLSGGMKQRLGLALALLHDPELLILDE 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 494 PTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLR--EDSYLN 561
Cdd:COG1131   158 PTSGLDPEARRELW-ELLRELAAEgkTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
337-553 5.59e-32

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: 131.14  E-value: 5.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:TIGR03375 466 FRNVSFAYpgqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVP 545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ--VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:TIGR03375 546 QDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLL 625
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR03375 626 DEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
337-537 6.09e-32

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: 120.81  E-value: 6.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQe 415
Cdd:cd00267     2 IENLSFRYgGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd00267    81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:cd00267   109 SGLDPASRERL-LELLRELAEEgrTVIIVTHDPELAELAADRVI 151
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
335-537 8.13e-32

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: 121.14  E-value: 8.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKS--IREHFAV 411
Cdd:cd03229     1 LELKNVSKRYgQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIF-NLSIRDNFKMLyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03229    81 VFQDFALFpHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 491 LDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIII 537
Cdd:cd03229   124 LDEPTSALDPITRREV-RALLKSLQAQlgiTVVLVTHDLDEAARLADRVV 172
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
342-536 4.37e-31

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: 121.14  E-value: 4.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK---NYDDLAEKSIREHFAVAFQEHHI 418
Cdd:cd03256    10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRRQIGMIFQQFNL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FN-LSIRDN-----------FKMLYENITDEEIYKSLEnvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:cd03256    90 IErLSVLENvlsgrlgrrstWRSLFGLFPKEEKQRALA---ALE---RVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDII 536
Cdd:cd03256   164 KLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLaREYADRIV 216
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
2-559 4.67e-31

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: 128.32  E-value: 4.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   2 VQILSNMIRPVVWSLLLAILVGTISTLSSISLMGLsawlIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKV 81
Cdd:TIGR01193 148 IPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKI----IDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  82 GFSLfTSFRVFVLIKIIKALPF-----KQQTENGDAFDLIVNAVDNLRDSFLRFFLP-PIITTISVFILsiwfFLYSYDL 155
Cdd:TIGR01193 224 GQRL-SIDIILSYIKHLFELPMsffstRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVGLFLV----RQNMLLF 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 156 MILLISSWLIFMIVIPYM--IWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQY---------QQ 224
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKrtFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYlnksfkyqkAD 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 225 YQQNLFKLKLKVNLcSEFIM--GAYLVICLAISIYLVntqdfnpimaitiiLTYQAvlevlammpsLIEHFDEASKRWQD 302
Cdd:TIGR01193 379 QGQQAIKAVTKLIL-NVVILwtGAYLVMRGKLTLGQL--------------ITFNA----------LLSYFLTPLENIIN 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 303 LAIFMQEKKFIANTNNEI---KSENQEDKQSKDVQLLLKDL-------AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGK 372
Cdd:TIGR01193 434 LQPKLQAARVANNRLNEVylvDSEFINKKKRTELNNLNGDIvindvsySYGYGSNILSDISLTIKMNSKTTIVGMSGSGK 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 373 STLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKM-LYENITDEEIYKSLENVYLLDF 451
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDD 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 452 VNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMeKYQKQTMIVTSHDISLL 529
Cdd:TIGR01193 594 IENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVA 672
                         570       580       590
                  ....*....|....*....|....*....|
gi 2674892663 530 RFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
349-547 8.27e-31

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: 119.92  E-value: 8.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE---KSIREHFAVAFQE-HHIFN--LS 422
Cdd:cd03257    21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRKEIQMVFQDpMSSLNprMT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDFVnQVGLDYIVGND-GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03257   101 IGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRyPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 502 TTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQG 547
Cdd:cd03257   180 VQAQIL-DLLKKLQEElglTLLFITHDLGVVAKIaDRVAVmyAG--KIVEEG 228
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
342-537 6.78e-30

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: 117.78  E-value: 6.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQEHH- 417
Cdd:TIGR02315  11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNl 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDN-----------FKMLYENITDEEIYKSLenvYLLDFVNQVGLDYIvgnDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:TIGR02315  91 IERLTVLENvlhgrlgykptWRSLLGRFSEEDKERAL---SALERVGLADKAYQ---RADQLSGGQQQRVAIARALAQQP 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIV 217
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
321-553 1.53e-29

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: 122.32  E-value: 1.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKDVQLLLKDLAYGY------DKVLLKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ 393
Cdd:COG1123   247 RGRAAPAAAAAEPLLEVRNLSKRYpvrgkgGVRAVDDVSLTLRRG-ETLgLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 394 GKNYDDLAEKSIRE---HFAVAFQE-HHIFN--LSIRD-------NFKMLYENITDEEIYKSLEnvylldfvnQVGLDYi 460
Cdd:COG1123   326 GKDLTKLSRRSLRElrrRVQMVFQDpYSSLNprMTVGDiiaeplrLHGLLSRAERRERVAELLE---------RVGLPP- 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 461 vgNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF- 532
Cdd:COG1123   396 --DLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL-NLLRDLQRElglTYLFISHDLAVVRYIa 472
                         250       260
                  ....*....|....*....|.
gi 2674892663 533 DDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1123   473 DRVAVMYDGRIVEDGPTEEVF 493
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
342-549 5.32e-29

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: 112.88  E-value: 5.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQEHhifnl 421
Cdd:cd03230    10 YG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEEP----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 sirdnfkMLYENITdeeiykslenvylldfvnqvGLDYIvgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03230    83 -------SLYENLT--------------------VRENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 502 TTNNIcSQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIicgeekIIEQGNI 549
Cdd:cd03230   130 SRREF-WELLRELKKEgkTILLSSHILEEAeRLCDRVA------ILNNGRI 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
335-555 3.19e-28

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: 118.47  E-value: 3.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDLAEKSIREH 408
Cdd:COG1123     5 LEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQE--HHIFNLSIRDN--FKMLYENITDEEIYKSLENvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAK 484
Cdd:COG1123    85 IGMVFQDpmTQLNPVTVGDQiaEALENLGLSRAEARARVLE--LLE---AVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEI-LDLLRELQRErgtTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA 233
cbiO PRK13637
energy-coupling factor transporter ATPase;
344-551 4.76e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 113.60  E-value: 4.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 344 YDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD--LAEKSIREHFAVAFQ--EHHIF 419
Cdd:PRK13637   18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypEYQLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGN--KLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13637   98 EETIEKDiaFGPINLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPT 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 496 AGLDIKTTNNICSQ---LMEKYqKQTMIVTSH---DISllRFFDDIIICGEEKIIEQGNIKK 551
Cdd:PRK13637  173 AGLDPKGRDEILNKikeLHKEY-NMTIILVSHsmeDVA--KLADRIIVMNKGKCELQGTPRE 231
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
338-559 4.83e-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: 118.77  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:COG5265   361 ENVSFGYDpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNfkMLY--ENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG5265   441 TVLFNDTIAYN--IAYgrPDASEEEVEAAARAAQIHDFIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:COG5265   519 DEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
332-553 6.02e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 113.40  E-value: 6.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIRE 407
Cdd:PRK13636    3 DYILKVEELNYNYSdgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13636   83 SVGMVFQdpDNQLFSASVYQDvsFGAVNLKLPEDEVRKRVDNA-----LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13636  158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVF 230
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
338-559 1.15e-27

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 117.90  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:TIGR00958 482 QDVSFSYpnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKtTNNICSQLMEKYQKqTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR00958 642 DEATSALDAE-CEQLLQESRSRASR-TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
341-559 1.80e-27

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 116.74  E-value: 1.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPL-KGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIF 419
Cdd:PRK10790  349 AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY-YPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVL 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKmLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:PRK10790  428 ADTFLANVT-LGRDISEEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 498 LDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:PRK10790  507 IDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
342-536 4.22e-27

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 110.15  E-value: 4.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH---FAVAFQEHHI 418
Cdd:COG3638    12 YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMIFQQFNL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 F-NLSIRDN-----------FKMLYENITDEEI---YKSLENVYLLDFVNQ-VGldyivgndgnKLSGGQKHRLQLAICL 482
Cdd:COG3638    92 VpRLSVLTNvlagrlgrtstWRSLLGLFPPEDReraLEALERVGLADKAYQrAD----------QLSGGQQQRVAIARAL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDII 536
Cdd:COG3638   162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLaRRYADRII 218
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
337-547 1.01e-26

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: 109.85  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD------KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN---YDDLAEKSIRE 407
Cdd:TIGR04521   3 LKNVSYIYQpgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDitaKKKKKLKDLRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRD-------NFKMlyeniTDEEI----YKSLEnvylldfvnQVGLDY-IVGNDGNKLSGGQK 473
Cdd:TIGR04521  83 KVGLVFQfpEHQLFEETVYKdiafgpkNLGL-----SEEEAeervKEALE---------LVGLDEeYLERSPFELSGGQM 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEdVAEYADRVIVMHKGKIVLDG 225
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
334-525 1.06e-26

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: 107.56  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEkSIREHFAVA 412
Cdd:COG4133     2 MLEAENLSCRRgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN----FKMLYENITDEEIYKSLENVYLLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICLAKQKD 487
Cdd:COG4133    81 GHADGLKpELTVRENlrfwAALYGLRADREAIDEALEAVGLAGL-----ADLPVRQ----LSAGQKRRVALARLLLSPAP 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDiKTTNNICSQLMEKYQKQ--TMIVTSHD 525
Cdd:COG4133   152 LWLLDEPFTALD-AAGVALLAELIAAHLARggAVLLTTHQ 190
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
335-547 1.36e-26

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: 107.61  E-value: 1.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAF 413
Cdd:cd03259     1 LELKGLSKTYGSVrALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03259    79 QDYALFpHLTVAENiaFGLKLRGVPKAEIRARVRELLEL-----VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLmEKYQKQ---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03259   154 LDEPLSALDAKLREELREEL-KELQRElgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
348-537 1.67e-26

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: 106.78  E-value: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehFAVAFQEHHIFNLSIRDN- 426
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENi 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 -FKMLYenitDEEIYKS-LENVYLL-DFVNQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03250    87 lFGKPF----DEERYEKvIKACALEpDLEILPDGDlTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNI-----CSQLMEkyqKQTMIVTSHDISLLRFFDDIII 537
Cdd:cd03250   163 GRHIfenciLGLLLN---NKTRILVTHQLQLLPHADQIVV 199
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
347-555 1.88e-26

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: 107.67  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQEhhiFNLSi 423
Cdd:cd03258    19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrRIGMIFQH---FNLL- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 rdNFKMLYENIT---------DEEIYKSLENvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:cd03258    95 --SSRTVFENVAlpleiagvpKAEIEERVLE--LLEL---VGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03258   168 TSALDPETTQSIL-ALLRDINRElglTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEEVFAN 231
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
335-558 4.57e-26

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 106.38  E-value: 4.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDkVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL--AEKSIrehfAVA 412
Cdd:COG3840     2 LRLDDLTYRYG-DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAERPV----SML 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDNF------KMlyeNITDEEIYKslenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ 485
Cdd:COG3840    77 FQENNLFPhLTVAQNIglglrpGL---KLTAEQRAQ------VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 486 KDIILLDEPTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:COG3840   148 RPILLLDEPFSALDpalrqemLDLVDELCRE-----RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEP 222

                  .
gi 2674892663 558 S 558
Cdd:COG3840   223 P 223
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
340-530 6.26e-26

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 105.90  E-value: 6.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEH 416
Cdd:COG2884     9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRRIGVVFQDF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 H-IFNLSIRDN--FKMLYENITDEEIYKSLENVylLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG2884    89 RlLPDRTVYENvaLPLRVTGKSRKEIRRRVREV--LD---LVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674892663 494 PTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLLR 530
Cdd:COG2884   164 PTGNLDPETSWEIM-ELLEEINRRgtTVLIATHDLELVD 201
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
337-537 7.32e-26

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: 105.30  E-value: 7.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDL--AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK--SIREHFAVA 412
Cdd:cd03262     3 IKNLhkSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKM-------LYENITDEEIYKSLENVYLLDFVNQvgldYIvgndgNKLSGGQKHRLQLAICLAK 484
Cdd:cd03262    82 FQQFNLFpHLTVLENITLapikvkgMSKAEAEERALELLEKVGLADKADA----YP-----AQLSGGQQQRVAIARALAM 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 485 QKDIILLDEPTAGLD---IKTTNNICSQLMEkyQKQTMIVTSHDISLLR-------FFDDIII 537
Cdd:cd03262   153 NPKVMLFDEPTSALDpelVGEVLDVMKDLAE--EGMTMVVVTHEMGFARevadrviFMDDGRI 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
337-544 1.05e-25

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: 104.65  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDKV--LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddLAEKSIREHFAVAFQ 414
Cdd:cd03226     2 IENISFSYKKGteILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 E--HHIFNLSIRD----NFKMLYENITD-EEIYKSLEnvyLLDFVNQVGLDyivgndgnkLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03226    79 DvdYQLFTDSVREelllGLKELDAGNEQaETVLKDLD---LYALKERHPLS---------LSGGQKQRLAIAAALLSGKD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKII 544
Cdd:cd03226   147 LLIFDEPTSGLDYKNMERVG-ELIRELAAQgkAVIVITHDYEFLaKVCDRVLLLANGAIV 205
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
338-543 2.26e-25

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 104.48  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03248    15 QNVTFAYptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVN--QVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03248    95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISelASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKI 543
Cdd:cd03248   175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
349-547 2.47e-25

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: 103.65  E-value: 2.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03369    24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MlYENITDEEIYKSLEnvylldfvnqvgldyiVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICS 508
Cdd:cd03369   104 P-FDEYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674892663 509 QLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03369   167 TIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
339-524 2.85e-25

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 105.12  E-value: 2.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YD---DLAEksIREHF 409
Cdd:COG1117    18 NVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDiYDpdvDVVE--LRRRV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFNLSIrdnfkmlYENIT--------------DEEIYKSLENVYLLDFV----NQVGLdyivgndgnKLSGG 471
Cdd:COG1117    95 GMVFQKPNPFPKSI-------YDNVAyglrlhgikskselDEIVEESLRKAALWDEVkdrlKKSAL---------GLSGG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ-TMIVTSH 524
Cdd:COG1117   159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIE-ELILELKKDyTIVIVTH 211
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
345-526 2.89e-25

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: 103.74  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQEHHIF-NLS 422
Cdd:cd03263    14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDrKAARQSLGYCPQFDALFdELT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDN------FKMLYENITDEEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03263    92 VREHlrfyarLKGLPKSEIKEEVELLLRVLGLTDKANkRAR----------TLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQKQTMIVTSHDI 526
Cdd:cd03263   162 SGLDPASRRAIWDLILEVRKGRSIILTTHSM 192
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
335-527 8.44e-25

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: 102.55  E-value: 8.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlAEKSIREHF 409
Cdd:cd03293     1 LEVRNVSKTYGggggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFN-LSIRDNFKMLYE--NITDEEIYKslenvYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARE-----RAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDIS 527
Cdd:cd03293   151 DVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDID 193
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
345-553 9.68e-25

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: 103.34  E-value: 9.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE-------HH 417
Cdd:COG1124    17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaslhpRH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKMLYENITDEEIYKSLEnvylldfvnQVGLD------YIvgndgNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG1124    97 TVDRILAEPLRIHGLPDREERIAELLE---------QVGLPpsfldrYP-----HQLSGGQRQRVAIARALILEPELLLL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1124   163 DEPTSALDVSVQAEIL-NLLKDLREErglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLL 227
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
338-552 1.33e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 103.62  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAF 413
Cdd:PRK13639    5 RDLKYSYPDgtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVGIVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRDN--FKMLYENITDEEIYK----SLENVYLLDFVNQVGldyivgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK13639   85 QnpDDQLFAPTVEEDvaFGPLNLGLSKEEVEKrvkeALKAVGMEGFENKPP---------HHLSGGQKKRVAIAGILAMK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13639  156 PEIIVLDEPTSGLDPMGASQI-MKLLYDLNKEgiTIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
334-564 3.62e-24

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: 102.24  E-value: 3.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYpLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:cd03289     2 QMTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03289    81 VIPQKVFIFSGTFRKNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIsllrffDDIIICGEEKIIEQGNIKKL-----LLREDSYLNKL 563
Cdd:cd03289   160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI------EAMLECQRFLVIEENKVRQYdsiqkLLNEKSHFKQA 233

                  .
gi 2674892663 564 I 564
Cdd:cd03289   234 I 234
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
342-528 1.05e-23

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: 99.40  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEHH- 417
Cdd:cd03292    10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIGVVFQDFRl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03292    90 LPDRNVYENvaFALEVTGVPPREIRKRVPAA-----LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISL 528
Cdd:cd03292   165 GNLDPDTTWEI-MNLLKKINKAgtTVVVATHAKEL 198
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
334-565 1.43e-23

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: 99.98  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:cd03288    19 EIKIHDLCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03288    99 IILQDPILFSGSIRFNLDP-ECKCTDDRLWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:cd03288   178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
347-553 1.54e-23

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: 105.80  E-value: 1.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDN 426
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  427 FKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:TIGR00957 1380 LDP-FSQYSDEEVWWALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2674892663  505 NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
337-547 2.30e-23

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 98.91  E-value: 2.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDL--AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD----DLAEksIREHFA 410
Cdd:COG1126     4 IENLhkSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINK--LRRKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIF-NLSIRdnfkmlyENIT-----------DEEIYKSLEnvyLLDfvnQVGLdyivgndGNK-------LSGG 471
Cdd:COG1126    81 MVFQQFNLFpHLTVL-------ENVTlapikvkkmskAEAEERAME---LLE---RVGL-------ADKadaypaqLSGG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLD----------IKttnnicsQLMEkyQKQTMIVTSHDISLLR-------FFDD 534
Cdd:COG1126   141 QQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldvMR-------DLAK--EGMTMVVVTHEMGFARevadrvvFMDG 211
                         250
                  ....*....|...
gi 2674892663 535 iiicGEekIIEQG 547
Cdd:COG1126   212 ----GR--IVEEG 218
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
331-553 2.48e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 99.68  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE 407
Cdd:PRK13632    4 KSVMIKVENVSFSYPnseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13632   84 KIGIIFQnpDNQFIGATVEDDIAFGLENkkVPPKKMKDIID-----DLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13632  159 LNPEIIIFDESTSMLDPKGKREI-KKIMVDLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
335-552 4.16e-23

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: 97.62  E-value: 4.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYdKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQ 414
Cdd:TIGR01277   1 LALDKVRYEY-EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDNFKMlyeNITDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:TIGR01277  78 ENNLFaHLTVRQNIGL---GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 494 PTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDISllrffDDIIICGEEKIIEQGNIKKL 552
Cdd:TIGR01277 155 PFSALDpllreemLALVKQLCSE-----RQRTLLMVTHHLS-----DARAIASQIAVVSQGKIKVV 210
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
335-549 8.58e-23

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: 95.36  E-value: 8.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV 411
Cdd:cd03246     1 LEVENVSFRYpgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03246    81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 492 DEPTAGLDIKTTNNICSQL-MEKYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNI 549
Cdd:cd03246   121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRIL------VLEDGRV 173
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
349-528 1.29e-22

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 95.57  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAFQ--EHHIFNLSIR 424
Cdd:TIGR01166   8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQdpDDQLFAADVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:TIGR01166  88 QDvaFGPLNLGLSEAEVERRVREALTA-----VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
                         170       180
                  ....*....|....*....|....*..
gi 2674892663 503 TNNICSQLME-KYQKQTMIVTSHDISL 528
Cdd:TIGR01166 163 REQMLAILRRlRAEGMTVVISTHDVDL 189
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
334-547 2.59e-22

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 96.62  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVA 412
Cdd:PRK11231    2 TLRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQeHHIFNLSI---------RDNFKMLYENITDEE---IYKSLENVYLLDFVNQVGLDyivgndgnkLSGGQKHRLQLAI 480
Cdd:PRK11231   82 PQ-HHLTPEGItvrelvaygRSPWLSLWGRLSAEDnarVNQAMEQTRINHLADRRLTD---------LSGGQRQRAFLAM 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICSqLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:PRK11231  152 VLAQDTPVVLLDEPTTYLDINHQVELMR-LMRELNTQgkTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
342-555 2.89e-22

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: 95.83  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIF-N 420
Cdd:cd03295    10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNF-------KMLYENItDEEIYKSLEnvylldfvnQVGLD--YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03295    90 MTVEENIalvpkllKWPKEKI-RERADELLA---------LVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03295   160 DEPFGALDPITRDQL-QEEFKRLQQElgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
325-545 3.87e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 100.14  E-value: 3.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVqLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfIQGKN----Ydd 399
Cdd:COG0488   307 PPERLGKKV-LELEGLSKSYgDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETvkigY-- 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 laeksirehFAvafQEHHIF--NLSIRDNFKMLYENITDEEIYKslenvYLLDFvnqvGLDyivGNDGNK----LSGGQK 473
Cdd:COG0488   383 ---------FD---QHQEELdpDKTVLDELRDGAPGGTEQEVRG-----YLGRF----LFS---GDDAFKpvgvLSGGEK 438
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDISLL-RFFDDIIICGEEKIIE 545
Cdd:COG0488   439 ARLALAKLLLSPPNVLLLDEPTNHLDIETL-----EALEEALDDfpgTVLLVSHDRYFLdRVATRILEFEDGGVRE 509
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
330-526 9.66e-22

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 94.77  E-value: 9.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGY-----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlAEKS 404
Cdd:COG1116     3 AAAPALELRGVSKRFptgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 405 IREHFAVAFQEHHIFN-LSIRDN--FKMLYENITDEEIYKSLEnvYLLDfvnQVGLdyivGNDGNK----LSGGQKHRLQ 477
Cdd:COG1116    78 PGPDRGVVFQEPALLPwLTVLDNvaLGLELRGVPKAERRERAR--ELLE---LVGL----AGFEDAyphqLSGGMRQRVA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMI-VTsHDI 526
Cdd:COG1116   149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLfVT-HDV 199
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
349-547 1.05e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 95.47  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFI------QGKNYDDLaeKSIREHFAVAFQ--EHHIFN 420
Cdd:PRK13634   23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL--KPLRKKVGIVFQfpEHQLFE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSI-RD------NFKMLYEnitdEEIYKSLENVYLldfvnqVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PRK13634  101 ETVeKDicfgpmNFGVSEE----DAKQKAREMIEL------VGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 493 EPTAGLDIKTTNNIcsqlME------KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13634  171 EPTAGLDPKGRKEM----MEmfyklhKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQG 228
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
330-553 1.39e-21

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: 94.63  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGYDK----------VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD 399
Cdd:cd03294    11 GKNPQKAFKLLAKGKSKeeilkktgqtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAEKSIRE----HFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIY----KSLENVYLLDFVNQvgldYIvgndgNKL 468
Cdd:cd03294    91 MSRKELRElrrkKISMVFQSFALLpHRTVLENvaFGLEVQGVPRAEREeraaEALELVGLEGWEHK----YP-----DEL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHD-ISLLRFFDDIIICGEEKIIE 545
Cdd:cd03294   162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241

                  ....*...
gi 2674892663 546 QGNIKKLL 553
Cdd:cd03294   242 VGTPEEIL 249
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
349-547 1.49e-21

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: 93.13  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIK---KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF- 419
Cdd:cd03297    10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFp 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRdnfkmlyENItdEEIYKSLENVYLLDFVNQV----GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03297    89 HLNVR-------ENL--AFGLKRKRNREDRISVDELldllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 496 AGLDiKTTNNICSQLMEKYQKQ---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03297   160 SALD-RALRLQLLPELKQIKKNlniPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
332-526 2.10e-21

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 94.08  E-value: 2.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YD-DLAEK 403
Cdd:PRK14243    8 ETVLRTENLNVYYGSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPgfrVEGKVTFHGKNlYApDVDPV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQEHHIFNLSIRDNFKML-----YENITDEEIYKSLENVYLLDFV----NQVGLdyivgndgnKLSGGQKH 474
Cdd:PRK14243   88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaringYKGDMDELVERSLRQAALWDEVkdklKQSGL---------SLSGGQQQ 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDI 526
Cdd:PRK14243  159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
189-537 3.31e-21

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 98.56  E-value: 3.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  189 TQEIIE-FYEGNRELSFYNYDKYRLKNINHSIEQYQQY--QQNLFKlKLKVNLCSEFIMGAY---------LVICLAISI 256
Cdd:PTZ00265   235 TMSIIEeALVGIRTVVSYCGEKTILKKFNLSEKLYSKYilKANFME-SLHIGMINGFILASYafgfwygtrIIISDLSNQ 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  257 YLVNtqDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDEASKRWQDLAIFMQEKKFIANtnneikseNQEDKQSKDVQ-L 335
Cdd:PTZ00265   314 QPNN--DFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN--------NDDGKKLKDIKkI 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  336 LLKDLAYGYDK----VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLAEKSIREHFA 410
Cdd:PTZ00265   384 QFKNVRFHYDTrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIG 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  411 VAFQEHHIFNLSIRDNFKML---------------------------------------------------------YEN 433
Cdd:PTZ00265   464 VVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknYQT 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  434 ITDEEIYKSLENVYLLDFVNQVGLDY--IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-------IKTTN 504
Cdd:PTZ00265   544 IKDSEVVDVSKKVLIHDFVSALPDKYetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylvQKTIN 623
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2674892663  505 NicsqlMEKYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PTZ00265   624 N-----LKGNENRITIIIAHRLSTIRYANTIFV 651
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
335-498 3.65e-21

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: 92.11  E-value: 3.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVA 412
Cdd:cd03224     1 LEVENLNAGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKMLYENITDEEIYKSLENVY-----LLDFVNQVGldyivGNdgnkLSGGQkhRLQLAIC--LAK 484
Cdd:cd03224    81 PEGRRIFpELTVEENLLLGAYARRRAKRKARLERVYelfprLKERRKQLA-----GT----LSGGE--QQMLAIAraLMS 149
                         170
                  ....*....|....
gi 2674892663 485 QKDIILLDEPTAGL 498
Cdd:cd03224   150 RPKLLLLDEPSEGL 163
cbiO PRK13646
energy-coupling factor transporter ATPase;
344-563 5.05e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.31  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 344 YDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQG----KNYDDLAEKSIREHFAVAFQ--EHH 417
Cdd:PRK13646   18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIR-------DNFKMLYENITDeeiykslenvYLLDFVNQVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK13646   98 LFEDTVEreiifgpKNFKMNLDEVKN----------YAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 490 LLDEPTAGLDIKTTNNICSqLMEKYQ---KQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKlLLREDSYLNKL 563
Cdd:PRK13646  168 VLDEPTAGLDPQSKRQVMR-LLKSLQtdeNKTIILVSHDMNeVARYADEVIVMKEGSIVSQTSPKE-LFKDKKKLADW 243
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
334-564 5.32e-21

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: 97.67  E-value: 5.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  334 QLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:TIGR01271 1217 QMDVQGLTAKYTeagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFG 1295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDP-YEQWSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663  489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKlLLREDSYLNKLI 564
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK-LLNETSLFKQAM 1449
cbiO PRK13640
energy-coupling factor transporter ATPase;
330-547 8.92e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 92.56  E-value: 8.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDLAEK 403
Cdd:PRK13640    1 MKDNIVEFKHVSFTYpdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVylldfVNQVG-LDYIVGNDGNkLSGGQKHRLQL 478
Cdd:PRK13640   81 DIREKVGIVFQnpDNQFVGATVGDDVAFGLENraVPRPEMIKIVRDV-----LADVGmLDYIDSEPAN-LSGGQKQRVAI 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICS---QLMEKYQkQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13640  155 AGILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNN-LTVISITHDIDEANMADQVLVLDDGKLLAQG 225
PLN03130 PLN03130
ABC transporter C family member; Provisional
349-565 9.79e-21

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 97.12  E-value: 9.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:PLN03130  1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  429 MLYENiTDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:PLN03130  1335 PFNEH-NDADLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663  507 CSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PLN03130  1414 QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
337-557 1.38e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 91.72  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:PRK13647    7 VEDLHFRYkdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 --EHHIFNLSIRDN--FKMLYENITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK13647   87 dpDDQVFSSTVWDDvaFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNiKKLLLRED 557
Cdd:PRK13647  162 LDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
345-553 1.39e-20

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: 91.30  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGN-IFIQGKNYD--DLAEksIREHFAV---AFQEHHI 418
Cdd:COG1119    15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGgeDVWE--LRKRIGLvspALQLRFP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDnfkM----------LYENITDEEIYKSLEnvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG1119    93 RDETVLD---VvlsgffdsigLYREPTDEQRERARE---LLEL---LGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDIKTT---NNICSQLMEKYQKQTMIVTsHDIS-LLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1119   164 LILDEPTAGLDLGARellLALLDKLAAEGAPTLVLVT-HHVEeIPPGITHVLLLKDGRVVAAGPKEEVL 231
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
335-536 1.51e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 91.61  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAV 411
Cdd:PRK13638    2 LATSDLWFRYqDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK13638   82 VFQdpEQQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEALTL-----VDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:PRK13638  157 YLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAV 206
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
335-536 1.65e-20

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 90.54  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:PRK10247    8 LQLQNVGYLAGdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYE--NITDEEiykslenVYLLDFVNQVGL-DYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK10247   88 QTPTLFGDTVYDNLIFPWQirNQQPDP-------AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLD---IKTTNNICSQLMEKYQKQTMIVTsHDISLLRFFDDII 536
Cdd:PRK10247  161 LDEITSALDesnKHNVNEIIHRYVREQNIAVLWVT-HDKDEINHADKVI 208
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
340-555 2.41e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 90.74  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:PRK14247   11 VSFGQVEVL-DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIELRRRVQMVFQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDNFKM------LYENITD--EEIYKSLENVYLLDFVNQvGLDYIVGndgnKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK14247   90 iPNPIPNLSIFENVALglklnrLVKSKKElqERVRWALEKAQLWDEVKD-RLDAPAG----KLSGGQQQRLCIARALAFQ 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSH-DISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:PRK14247  165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
342-547 3.27e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 90.07  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLkDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD---DLAEKSIRE---HFAVAFQE 415
Cdd:PRK11124   12 YGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRElrrNVGMVFQQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNF-----KM--LYENITDEEIYKSLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK11124   91 YNLWpHLTVQQNLieapcRVlgLSKDQALARAEKLLERLRLKPYADRFPL---------HLSGGQQQRVAIARALMMEPQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDIIICGEE-KIIEQG 547
Cdd:PRK11124  162 VLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYMENgHIVEQG 223
cbiO PRK13645
energy-coupling factor transporter ATPase;
330-548 4.29e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 90.84  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVqlLLKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQG----KNYDD 399
Cdd:PRK13645    4 SKDI--ILDNVSYTYAKKTpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE-KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLENvyLLDFVnQVGLDYiVGNDGNKLSGGQKH 474
Cdd:PRK13645   82 IKEvKRLRKEIGLVFQfpEYQLFQETIEKDiaFGPVNLGENKQEAYKKVPE--LLKLV-QLPEDY-VKRSPFELSGGQKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTN---NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK13645  158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
PLN03232 PLN03232
ABC transporter C family member; Provisional
348-565 5.03e-20

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 94.66  E-value: 5.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNF 427
Cdd:PLN03232  1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  428 KMLYENiTDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:PLN03232  1331 DPFSEH-NDADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  506 ICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PLN03232  1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
335-526 6.21e-20

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 88.87  E-value: 6.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVLLKdINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQ 414
Cdd:PRK10771    2 LKLTDITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIFN-LSIRDNFKM-LYENIT-DEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK10771   79 ENNLFShLTVAQNIGLgLNPGLKlNAAQREKLH-----AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDI 526
Cdd:PRK10771  154 DEPFSALDpalrqemLTLVSQVCQE-----RQLTLLMVSHSL 190
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
335-525 6.29e-20

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: 88.47  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL--AEKSIrehfAV 411
Cdd:cd03301     1 VELENVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppKDRDI----AM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03301    77 VFQNYALYpHMTVYDNiaFGLKLRKVPKDEIDERVREVAEL-----LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHD 525
Cdd:cd03301   152 FLMDEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHD 190
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
340-556 8.15e-20

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 89.28  E-value: 8.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ----- 414
Cdd:PRK10253   15 LGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnattp 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDNF--KMLYENITDEEiykslenvylLDFVNQ----VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK10253   94 gDITVQELVARGRYphQPLFTRWRKED----------EEAVTKamqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRE 556
Cdd:PRK10253  164 IMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
337-532 1.22e-19

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 92.05  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--------NYDDLAEKSIRE 407
Cdd:COG0488     1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDLTVLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQEhhifNLSIRDNFKMLYENITDEEI----YKSLENVY--------------LLDfvnqvGLDyIVGNDGNK-- 467
Cdd:COG0488    81 TVLDGDAE----LRALEAELEELEAKLAEPDEdlerLAELQEEFealggweaearaeeILS-----GLG-FPEEDLDRpv 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 468 --LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFF 532
Cdd:COG0488   151 seLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-----EWLEEFLKNypgTVLVVSHD----RYF 211
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
349-537 1.40e-19

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: 87.91  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--------------NYDDLAEKSIREHFAVAfq 414
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmvvfqNYSLLPWLTVRENIALA-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 ehhiFNLSIRDNFKMLYENITDEEIykslenvylldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:TIGR01184  79 ----VDRVLPDLSKSERRAIVEEHI-------------ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVV 186
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
351-553 1.56e-19

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: 89.73  E-value: 1.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPL---KGNIFIQGKNYDDLAEKSIRE----HFAVAFQE-HHIFN- 420
Cdd:COG0444    23 GVSFDVRRG-ETLgLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpMTSLNp 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 -LSIRDNFK---MLYENITDEEIY-KSLEnvyLLDfvnQVGLDyivgnDGNK--------LSGGQKHRLQLAICLAKQKD 487
Cdd:COG0444   102 vMTVGDQIAeplRIHGGLSKAEAReRAIE---LLE---RVGLP-----DPERrldrypheLSGGMRQRVMIARALALEPK 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 488 IILLDEPTAGLDIkTTnnicsQ-----LMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQGNIKKLL 553
Cdd:COG0444   171 LLIADEPTTALDV-TI-----QaqilnLLKDLQRElglAILFITHDLGVVAEIaDRVAVmyAG--RIVEEGPVEELF 239
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
340-536 1.75e-19

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: 87.39  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD--LAEKSIREHFAVAF--QE 415
Cdd:cd03290     8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsFEATRSRNRYSVAYaaQK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNfkMLYENITDEEIYK------SLE-NVYLLDFVNQVGldyiVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03290    88 PWLLNATVEEN--ITFGSPFNKQRYKavtdacSLQpDIDLLPFGDQTE----IGERGINLSGGQRQRICVARALYQNTNI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKY---QKQTMIVTSHDISLLRFFDDII 536
Cdd:cd03290   162 VFLDDPFSALDIHLSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWII 212
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
349-559 2.03e-19

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: 87.39  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaeKSIREHFAVAFQEHHIF-NLSIRDN- 426
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFpHMTVYKNi 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 -FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:cd03299    93 aYGLKKRKVDKKEIERKVLEI-----AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 506 ICSQLME--KYQKQTMIVTSHDisllrfFDDIIICGEE-------KIIEQGNIKKLLLREDSY 559
Cdd:cd03299   168 LREELKKirKEFGVTVLHVTHD------FEEAWALADKvaimlngKLIQVGKPEEVFKKPKNE 224
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
346-557 2.35e-19

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: 91.64  E-value: 2.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRD 425
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAE 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKMLYENITDEEIYKS--LENVY--LLDFVNqvGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:TIGR01842 411 NIARFGENADPEKIIEAakLAGVHelILRLPD--GYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 502 TTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNIKKLLLRED 557
Cdd:TIGR01842 489 GEQALANAIKAlKARGITVVVITHRPSLLGCVDKIL------VLQDGRIARFGERDE 539
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
335-554 2.39e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 87.91  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YDDLAEK-SIR 406
Cdd:PRK14239    6 LQVSDLSVYYnKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNiYSPRTDTvDLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHHIFNLSIRDNfkMLY---------ENITDEEIYKSLENVYLLDFVNQVGLDYIVGndgnkLSGGQKHRLQ 477
Cdd:PRK14239   86 KEIGMVFQQPNPFPMSIYEN--VVYglrlkgikdKQVLDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:PRK14239  159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFM 236
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
349-538 2.85e-19

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: 87.11  E-value: 2.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH-FAVAFQEHHIF-NLSIRDN 426
Cdd:cd03219    16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFpELTVLEN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 ------------FKMLYENITDEEIYKSLENvyLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03219    96 vmvaaqartgsgLLLARARREEREARERAEE--LLERV---GLadlaDRPAGE----LSYGQQRRLEIARALATDPKLLL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDIIIC 538
Cdd:cd03219   167 LDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTV 215
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
341-525 2.88e-19

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: 86.91  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQEHHIF- 419
Cdd:cd03300     9 FYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFp 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN------FKMLYENITDEEIYKSLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03300    86 HLTVFENiafglrLKKLPKAEIKERVAEALDLVQLEGYANR---------KPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 494 PTAGLDIKTTNNICSQLMEkYQKQ---TMIVTSHD 525
Cdd:cd03300   157 PLGALDLKLRKDMQLELKR-LQKElgiTFVFVTHD 190
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
283-568 4.27e-19

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: 91.93  E-value: 4.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  283 LAMMPSLIEHFDEASKRWQDLAIFMQEKkfiantnnEIKSENQEDKQSKD---VQLLLKDLAYGYDKVL---LKDINLSI 356
Cdd:TIGR00957  590 LNILPMVISSIVQASVSLKRLRIFLSHE--------ELEPDSIERRTIKPgegNSITVHNATFTWARDLpptLNGITFSI 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyddlaeksirehfAVAF--QEHHIFNLSIRDNfkMLYENI 434
Cdd:TIGR00957  662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------SVAYvpQQAWIQNDSLREN--ILFGKA 724
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  435 TDEEIYKS-LENVYLL-DFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL- 510
Cdd:TIGR00957  725 LNEKYYQQvLEACALLpDLEILPSGDRTeIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVi 804
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  511 --MEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIRYKN 568
Cdd:TIGR00957  805 gpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
337-547 4.68e-19

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 87.38  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKS---IREHFA 410
Cdd:PRK13635    8 VEHISFRYpdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETvwdVRRQVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:PRK13635   85 MVFQnpDNQFVGATVQDDVAFGLENigVPREEMVERVD-----QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISLLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13635  160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSitHDLDEAAQADRVIVMNKGEILEEG 222
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
335-525 7.49e-19

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 88.23  E-value: 7.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLY----PLKGNIFIQGKNYDDL-AEKsiReH 408
Cdd:COG3842     6 LELENVSKRYGDVTaLDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetPDSGRILLDGRDVTGLpPEK--R-N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIF-NLSIRDN--F--KMLyeNITDEEIYKSLENvyLLDfvnQVGLD-----YIvgndgNKLSGGQKHRLQL 478
Cdd:COG3842    79 VGMVFQDYALFpHLTVAENvaFglRMR--GVPKAEIRARVAE--LLE---LVGLEgladrYP-----HQLSGGQQQRVAL 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEkYQKQ---TMI-VTsHD 525
Cdd:COG3842   147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRR-LQRElgiTFIyVT-HD 195
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
342-547 9.07e-19

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: 84.96  E-value: 9.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRehfAVAFQEHHIF-- 419
Cdd:cd03268    10 YG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGALIEAPGFyp 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKM--LYENITDEEIYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:cd03268    86 NLTARENLRLlaRLLGIRKKRIDEVLD---------VVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 498 LDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03268   157 LDPDGIKEL-RELILSLRDQgiTVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
343-553 9.32e-19

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 89.77  E-value: 9.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PRK10789  325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIykslENVYLLDFVNQ------VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:PRK10789  405 VANNIALGRPDATQQEI----EHVARLASVHDdilrlpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 497 GLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK10789  481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
349-553 1.34e-18

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 88.17  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE----HFAVAFQEHHIF-NLSI 423
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDN--FKMLYENITDEEIYKSlenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-- 499
Cdd:PRK10070  124 LDNtaFGMELAGINAEERREK-----ALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpl 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 IKT-TNNICSQLMEKYQKqTMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK10070  199 IRTeMQDELVKLQAKHQR-TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
346-553 1.36e-18

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: 86.01  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREHFAVAFQE-HHIFN- 420
Cdd:TIGR02769  24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNp 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 -LSIRDNFKMLYENITDeeIYKSLENVYLLDFVNQVGLDyivGNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR02769 104 rMTVRQIIGEPLRHLTS--LDESEQKARIAELLDMVGLR---SEDADKlprqLSGGQLQRINIARALAVKPKLIVLDEAV 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 496 AGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR02769 179 SNLDMVLQAVIL-ELLRKLQQAfgtAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLL 239
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
349-501 1.59e-18

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: 85.08  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE-HFAVAFQEHHIF-NLSIRDN 426
Cdd:cd03296    18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDVPVQErNVGFVFQHYALFrHMTVFDN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F------KMLYENITDEEIYKSLENvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:cd03296    95 VafglrvKPRSERPPEAEIRAKVHE--LLKL---VQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169

                  .
gi 2674892663 501 K 501
Cdd:cd03296   170 K 170
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
345-558 1.60e-18

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 87.08  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyDDLAEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:PRK11432   18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFpHMS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDN----FKMLyeNITDEEIYKSL-ENVYLLD-------FVNQVgldyivgndgnklSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK11432   95 LGENvgygLKML--GVPKEERKQRVkEALELVDlagfedrYVDQI-------------SGGQQQRVALARALILKPKVLL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 491 LDEPTAGLDIkttnNICSQLMEK---YQKQ---TMIVTSHDISllRFF---DDIIICGEEKIIEQGNIKKLLLREDS 558
Cdd:PRK11432  160 FDEPLSNLDA----NLRRSMREKireLQQQfniTSLYVTHDQS--EAFavsDTVIVMNKGKIMQIGSPQELYRQPAS 230
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
349-555 2.53e-18

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 86.29  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQehHiFNL---- 421
Cdd:COG1135    21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrKIGMIFQ--H-FNLlssr 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLENvyLLDFVnqvGLdyivgndGNK-------LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG1135    98 TVAENvaLPLEIAGVPKAEIRKRVAE--LLELV---GL-------SDKadaypsqLSGGQKQRVGIARALANNPKVLLCD 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 493 EPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDIsllrffdDII--IC--------GeeKIIEQGNIKKLLLR 555
Cdd:COG1135   166 EATSALDPETTRSIL-DLLKDINRElglTIVLITHEM-------DVVrrICdrvavlenG--RIVEQGPVLDVFAN 231
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
351-547 3.39e-18

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: 83.31  E-value: 3.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD--DLAEKSIrehfAVAFQEHHIF-NLSIRDNF 427
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaaPPADRPV----SMLFQENNLFaHLTVEQNV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 428 KM-----LYENITDEEIYKSLenvylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03298    92 GLglspgLKLTAEDRQAIEVA--------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2674892663 503 TNNICSQLMEKYQKQTM---IVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03298   164 RAEMLDLVLDLHAETKMtvlMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
342-548 3.82e-18

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 83.91  E-value: 3.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD---DLAEKSIRE---HFAVAFQE 415
Cdd:COG4161    12 YGSHQAL-FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLlrqKVGMVFQQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNF-----KMLYEN--ITDEEIYKSLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKD 487
Cdd:COG4161    91 YNLWpHLTVMENLieapcKVLGLSkeQAREKAMKLLARLRLTDKADRFPL---------HLSGGQQQRVAIARALMMEPQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDIIICGEE-KIIEQGN 548
Cdd:COG4161   162 VLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKgRIIEQGD 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
331-547 3.88e-18

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: 82.60  E-value: 3.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQGKNYDdlaEKSIREH 408
Cdd:cd03213     7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQE-HHIFNLSIRDNfkmlyenitdeeiykslenvylldfvnqvgLDYIVGNDGnkLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03213    84 IGYVPQDdILHPTLTVRET------------------------------LMFAAKLRG--LSGGERKRVSIALELVSNPS 131
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 488 IILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03213   132 LLFLDEPTSGLDSSSALQV-MSLLRRLADTgrTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
337-542 4.93e-18

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: 80.96  E-value: 4.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaeksirehfavafqe 415
Cdd:cd03221     3 LENLSKTYgGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeEIYKSLENVYLldfvnqvgldyivgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03221    58 ----------------------TWGSTVKIGYF-----------------EQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 496 AGLDIKTtnniCSQLME--KYQKQTMIVTSHDISLL-RFFDDIIICGEEK 542
Cdd:cd03221    99 NHLDLES----IEALEEalKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
345-547 6.57e-18

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: 83.09  E-value: 6.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKnydDLAEKSIREHFAVAFQeHHIF-- 419
Cdd:cd03234    19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPDQFQKCVAYVRQ-DDILlp 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRD------NFKMLYENiTDEEIYKSLENVYLLDFVN-QVGLDYIVGndgnkLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:cd03234    95 GLTVREtltytaILRLPRKS-SDAIRKKRVEDVLLRDLALtRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 493 EPTAGLDIKTTNNIC---SQLMEKyqKQTMIVTSHD--ISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03234   169 EPTSGLDSFTALNLVstlSQLARR--NRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
349-552 8.69e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 84.11  E-value: 8.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK----NYDDLAEKSIREHFAVAFQ--EHHIF-NL 421
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFeNT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRD-NFKMLYENITDEEIYKSLenvylLDFVNQVGLDYIVGNDGN-KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13641  103 VLKDvEFGPKNFGFSEDEAKEKA-----LKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 500 IKTTNNICsQLMEKYQK--QTMIVTSH---DISllRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13641  178 PEGRKEMM-QLFKDYQKagHTVILVTHnmdDVA--EYADDVLVLEHGKLIKHASPKEI 232
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
349-548 9.15e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 83.65  E-value: 9.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE-HHIFNLSI---- 423
Cdd:PRK13648   25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpDNQFVGSIvkyd 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 ----RDNFKMLYENITdEEIYKSLENVYLLDFVNqvgldyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13648  105 vafgLENHAVPYDEMH-RRVSEALKQVDMLERAD---------YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 500 IKTTNNICSQLME-KYQKQ-TMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK13648  175 PDARQNLLDLVRKvKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
342-552 1.09e-17

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 83.98  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQEHHIF- 419
Cdd:TIGR01188   3 YG-DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG--YDVVREpRKVRRSIGIVPQYASVDe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVNQVGLDYivgndgnklSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:TIGR01188  80 DLTGRENLEMmgrLYglpKDEAEERAEELLELFELGEAADRPVGTY---------SGGMRRRLDIAASLIHQPDVLFLDE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 494 PTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRAlKEEGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEEL 211
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
335-499 1.50e-17

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 82.00  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLA--YGYDKVLlKDINLSIKKGNktlIV---GTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSI--RE 407
Cdd:COG1137     4 LEAENLVksYGKRTVV-KDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DITHLPMhkRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAF--QEHHIF-NLSIRDNFKMLYE--NITDEEIYKSLENvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICL 482
Cdd:COG1137    77 RLGIGYlpQEASIFrKLTVEDNILAVLElrKLSKKEREERLEE--LLE---EFGITHLRKSKAYSLSGGERRRVEIARAL 151
                         170
                  ....*....|....*..
gi 2674892663 483 AKQKDIILLDEPTAGLD 499
Cdd:COG1137   152 ATNPKFILLDEPFAGVD 168
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
349-525 1.57e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 85.93  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHHIF-NLSI 423
Cdd:PRK10535   24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLsHLTA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKMlyenitdEEIYKSLENVYLL----DFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK10535  104 AQNVEV-------PAVYAGLERKQRLlraqELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
                         170       180
                  ....*....|....*....|....*....
gi 2674892663 500 IKTTN---NICSQLMEkyQKQTMIVTSHD 525
Cdd:PRK10535  177 SHSGEevmAILHQLRD--RGHTVIIVTHD 203
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
334-564 1.66e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 83.60  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE----- 402
Cdd:PRK13651    2 QIKVKNIVKIFNKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkeke 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 403 -------------------KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLenvylLDFVNQVGLD- 458
Cdd:PRK13651   82 kvleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDiiFGPVSMGVSKEEAKKRA-----AKYIELVGLDe 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 459 -YIVGNDGNkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDI-SLLRFFDDI 535
Cdd:PRK13651  157 sYLQRSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2674892663 536 IICGEEKIIEQGNIKKlLLREDSYL--NKLI 564
Cdd:PRK13651  236 IFFKDGKIIKDGDTYD-ILSDNKFLieNNME 265
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
351-557 2.68e-17

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: 83.62  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF-NLSIR 424
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEARLFpHLSVR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DNFKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:TIGR02142  94 GNLRYGMKRARPSERRISFERVIEL-----LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 505 NICSQLmEKYQKQT---MIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:TIGR02142 169 EILPYL-ERLHAEFgipILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
346-548 4.92e-17

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: 80.66  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaEKSIREHFAVAF--QEHHIF-NLS 422
Cdd:cd03218    13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARLGIGYlpQEASIFrKLT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03218    92 VEENILAVLEIRGLSKKEREEKLEELLE---EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNIcsQLMEKYQKQTMI---VTSHDIS-LLRFFDDIIICGEEKIIEQGN 548
Cdd:cd03218   169 VQDI--QKIIKILKDRGIgvlITDHNVReTLSITDRAYIIYEGKVLAEGT 216
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
348-528 5.27e-17

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 80.63  E-value: 5.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLGFIYQFHHLLpDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKM--LYENITDEEIYKSLenvylLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:PRK11629  104 ALENVAMplLIGKKKPAEINSRA-----LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
                         170       180       190
                  ....*....|....*....|....*....|
gi 2674892663 501 KTTNNICSQLMEKYQKQ--TMIVTSHDISL 528
Cdd:PRK11629  179 RNADSIFQLLGELNRLQgtAFLVVTHDLQL 208
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
342-553 6.24e-17

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 80.78  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN-------------YDDLAEKSIREH 408
Cdd:PRK10619   15 YGEHEVL-KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEhhiFNLSirdNFKMLYENITDEEIY-----KSLENVYLLDFVNQVGLDYIV-GNDGNKLSGGQKHRLQLAICL 482
Cdd:PRK10619   94 LTMVFQH---FNLW---SHMTVLENVMEAPIQvlglsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARAL 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 483 AKQKDIILLDEPTAGLD---IKTTNNICSQLMEkyQKQTMIVTSHDISLLRFFDD-IIICGEEKIIEQGNIKKLL 553
Cdd:PRK10619  168 AMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
349-533 7.55e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 80.70  E-value: 7.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddlAEKSIREHFAVAFQEHHIFNLSirdnFK 428
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQKNLVAYVPQSEEVDWS----FP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYENIT-----------------DEEIY-KSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK15056   95 VLVEDVVmmgryghmgwlrrakkrDRQIVtAALARVDMVEFRHrQIG----------ELSGGQKKRVFLARAIAQQGQVI 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDI-SLLRFFD 533
Cdd:PRK15056  165 LLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLgSVTEFCD 210
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
345-564 8.72e-17

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 80.18  E-value: 8.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDdlAEKSI----------REHFAVAFQ 414
Cdd:PRK11264   15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLsqqkglirqlRQHVGFVFQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EhhiFNLsirdnF--KMLYENIT-----------DEEIYKSLEnvylldFVNQVGLDYIVGNDGNKLSGGQKHRLQLAIC 481
Cdd:PRK11264   93 N---FNL-----FphRTVLENIIegpvivkgepkEEATARARE------LLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICS---QLMEkyQKQTMIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLLL--- 554
Cdd:PRK11264  159 LAMRPEVILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFAdpq 236
                         250
                  ....*....|..
gi 2674892663 555 --REDSYLNKLI 564
Cdd:PRK11264  237 qpRTRQFLEKFL 248
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
320-533 9.22e-17

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 83.32  E-value: 9.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDlaygyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLYPLKGNI- 390
Cdd:COG4178   355 IETSEDGALALEDLTLRTPD-----GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVl 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 391 FIQGKNYddLAEKSIREhfAVAFQEHHifnlsirdnfkmlyENITDEEIYKSLENVYLLDFVNQvgLDyiVGND-GNKLS 469
Cdd:COG4178   430 FLPQRPY--LPLGTLRE--ALLYPATA--------------EAFSDAELREALEAVGLGHLAER--LD--EEADwDQVLS 487
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 470 GGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFD 533
Cdd:COG4178   488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHD 551
PLN03232 PLN03232
ABC transporter C family member; Provisional
213-552 9.44e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 84.26  E-value: 9.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  213 KNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVICLAIS--IYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLI 290
Cdd:PLN03232   499 KSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSfgVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLL 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  291 EHFDEASKRWQDLA-IFMQEKKFIANtnneiksenQEDKQSKDVQLLLKDLAYGYD----KVLLKDINLSIKKGNKTLIV 365
Cdd:PLN03232   579 SQVVNANVSLQRIEeLLLSEERILAQ---------NPPLQPGAPAISIKNGYFSWDsktsKPTLSDINLEIPVGSLVAIV 649
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  366 GTSGCGKSTLFYVLMRLLYPLKGNIFIqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNfkMLYENITDEEIYKSLEN 445
Cdd:PLN03232   650 GGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVREN--ILFGSDFESERYWRAID 715
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  446 VYLLdfvnQVGLDYIVGND-------GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLM-EKYQKQ 517
Cdd:PLN03232   716 VTAL----QHDLDLLPGRDlteigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkDELKGK 791
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2674892663  518 TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PLN03232   792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
341-525 1.03e-16

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 82.00  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPLK----GNIFIQGKNYDDL--AEKSIrehfAVAFQ 414
Cdd:PRK11000   12 AYG-DVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGLEditsGDLFIGEKRMNDVppAERGV----GMVFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDN--FKMLYENITDEEIYKSlenvylldfVNQVG----LDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK11000   83 SYALYpHLSVAENmsFGLKLAGAKKEEINQR---------VNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLD----IKTTNNIcSQLMEKYQKqTMIVTSHD 525
Cdd:PRK11000  154 VFLLDEPLSNLDaalrVQMRIEI-SRLHKRLGR-TMIYVTHD 193
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
334-525 1.49e-16

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 81.27  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPL----KGNIFIQGKNYDDLAEKsiREH 408
Cdd:COG3839     3 SLELENVSKSYGGVEaLKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAGLedptSGEILIGGRDVTDLPPK--DRN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENV-------YLLD-FVNQvgldyivgndgnkLSGGQKHRLQ 477
Cdd:COG3839    77 IAMVFQSYALYpHMTVYENiaFPLKLRKVPKAEIDRRVREAaellgleDLLDrKPKQ-------------LSGGQRQRVA 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMeKYQKQ---TMI-VTsHD 525
Cdd:COG3839   144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIK-RLHRRlgtTTIyVT-HD 193
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
337-526 1.53e-16

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 79.36  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE---HFAVA 412
Cdd:COG4604     4 IKNVSKRYgGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL---DVATTPSRElakRLAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHI-FNLSIRDnfkmLYE---------NITDEE---IYKSLENVYLLDFVNQvgldYIvgndgNKLSGGQKHRLQLA 479
Cdd:COG4604    81 RQENHInSRLTVRE----LVAfgrfpyskgRLTAEDreiIDEAIAYLDLEDLADR----YL-----DELSGGQRQRAFIA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTtnniCSQLM-------EKYQKQTMIVTsHDI 526
Cdd:COG4604   148 MVLAQDTDYVLLDEPLNNLDMKH----SVQMMkllrrlaDELGKTVVIVL-HDI 196
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
342-524 1.70e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 79.50  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-----YPLKGNIFIQGKN--YDDLAEKSIREHFAVAFQ 414
Cdd:PRK14267   14 YGSNHVI-KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiySPDVDPIEVRREVGMVFQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDN--FKMLYENIT------DEEIYKSLENVYLLDFVNQVGLDYivgndGNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK14267   93 YPNPFpHLTIYDNvaIGVKLNGLVkskkelDERVEWALKKAALWDEVKDRLNDY-----PSNLSGGQRQRLVIARALAMK 167
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSH 524
Cdd:PRK14267  168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
345-555 1.74e-16

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 79.34  E-value: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLY-PLKGNIFIQGKNYDDL-AEKSIREHFAVAFQ---EhhI 418
Cdd:COG0396    12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgHPKYeVTSGSILLDGEDILELsPDERARAGIFLAFQypvE--I 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQVGLD------YIvgNDGnkLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG0396    90 PGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDedfldrYV--NEG--FSGGEKKRNEILQMLLLEPKLAILD 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 493 EPTAGLDI---KTTNNICSQLMEKyqKQTMIVTSHDISLLRFF--DDIIICGEEKIIEQGNiKKLLLR 555
Cdd:COG0396   166 ETDSGLDIdalRIVAEGVNKLRSP--DRGILIITHYQRILDYIkpDFVHVLVDGRIVKSGG-KELALE 230
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
338-557 1.93e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 79.85  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ- 414
Cdd:PRK13652    7 RDLCYSYsgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK13652   87 pDDQIFSPTVEQDiaFGPINLGLDEETVAHRVSSA-----LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNI---CSQLMEKYqKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:PRK13652  162 DEPTAGLDPQGVKELidfLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
335-498 1.99e-16

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: 78.87  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKSIREHFAVA 412
Cdd:COG0410     4 LEVENLHAGYGGIHvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKM-LYENITDEEIYKSLENVY-----LLDFVNQvgldyivgnDGNKLSGGQkhRLQLAIC--LA 483
Cdd:COG0410    84 PEGRRIFpSLTVEENLLLgAYARRDRAEVRADLERVYelfprLKERRRQ---------RAGTLSGGE--QQMLAIGraLM 152
                         170
                  ....*....|....*
gi 2674892663 484 KQKDIILLDEPTAGL 498
Cdd:COG0410   153 SRPKLLLLDEPSLGL 167
cbiO PRK13644
energy-coupling factor transporter ATPase;
337-553 2.36e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 79.65  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE-KSIREHFAVAF 413
Cdd:PRK13644    4 LENVSYSYpdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRDNFKMLYENIT--DEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK13644   84 QnpETQFVGRTVEEDLAFGPENLClpPIEIRKRVDRA-----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13644  159 IFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
317-565 2.43e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 83.15  E-value: 2.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  317 NNEIKSENQEDKQSKdvqLLLKDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLK----- 387
Cdd:PTZ00265  1151 NGGIRIKNKNDIKGK---IEIMDVNFRYisrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRF-YDLKndhhi 1226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  388 --------------------------------------------------GNIFIQGKNYDDLAEKSIREHFAVAFQEHH 417
Cdd:PTZ00265  1227 vfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPM 1306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  418 IFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PTZ00265  1307 LFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEAT 1386
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663  496 AGLDIKTTNNICSQLMEKYQK--QTMIVTSHDISLLRFFDDIIICGEEK-----IIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PTZ00265  1387 SSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKKYVK 1463
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
345-526 2.49e-16

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: 78.53  E-value: 2.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI----FIQGKNYDDLAEKsirehFAVAF--QEHHI 418
Cdd:cd03267    33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRR-----IGVVFgqKTQLW 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFKMLYE--NITDEEIYKSLEN-VYLLDfvnqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03267   108 WDLPVIDSFYLLAAiyDLPPARFKKRLDElSELLD------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2674892663 496 AGLDIKTTNNICSQLME--KYQKQTMIVTSHDI 526
Cdd:cd03267   182 IGLDVVAQENIRNFLKEynRERGTTVLLTSHYM 214
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
328-525 3.78e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 78.55  E-value: 3.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 328 KQSKDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL------YPLKGNIFIQGKNYDDLA 401
Cdd:PRK14246    5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQID 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 402 EKSIREHFAVAFQEHHIF-NLSIRDN--FKMLYENITDE-EIYKSLEnvyllDFVNQVGLDYIV----GNDGNKLSGGQK 473
Cdd:PRK14246   85 AIKLRKEVGMVFQQPNPFpHLSIYDNiaYPLKSHGIKEKrEIKKIVE-----ECLRKVGLWKEVydrlNSPASQLSGGQQ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHD 525
Cdd:PRK14246  160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHN 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
338-552 4.70e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 78.59  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY-------DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIqgKNYDDLAEKS---IRE 407
Cdd:PRK13633    8 KNVSYKYesneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENlwdIRN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13633   86 KAGMVFQnpDNQIVATIVEEDVAFGPENlgIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
335-547 6.45e-16

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: 76.85  E-value: 6.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDK-VLLKDINLSIKKGNKTLiVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAEKS-IREHFAVA 412
Cdd:cd03264     1 LQLENLTKRYGKkRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQkLRRRIGYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRD--NFKMLYENITD----EEIYKSLENVYLLDFVNqvglDYIvgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:cd03264    78 PQEFGVYpNFTVREflDYIAWLKGIPSkevkARVDEVLELVNLGDRAK----KKI-----GSLSGGMRRRVGIAQALVGD 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:cd03264   149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
338-552 6.55e-16

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: 77.02  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQE 415
Cdd:cd03265     4 ENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREpREVRRRIGIVFQD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFN-LSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVnqvglDYIVGNdgnkLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03265    82 LSVDDeLTGWENLYIharLYgvpGAERRERIDELLDFVGLLEAA-----DRLVKT----YSGGMRRRLEIARSLVHRPEV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:cd03265   153 LFLDEPTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
343-538 1.01e-15

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 75.73  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaekSIREHFAVAFQEHHI--- 418
Cdd:NF040873    1 GYGgRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVPQRSevp 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 --FNLSIRDNFKM-------LYENITDE---EIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQ 485
Cdd:NF040873   68 dsLPLTVRDLVAMgrwarrgLWRRLTRDdraAVDDALERVGLADLAGrQLG----------ELSGGQRQRALLAQGLAQE 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLM--EKYQKQTMIVTSHDISLLRFFDDIIIC 538
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERI-IALLaeEHARGATVVVVTHDLELVRRADPCVLL 191
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
345-547 1.08e-15

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: 76.17  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAeksiREHFAVAFQEHHIF-NLSI 423
Cdd:cd03269    12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKMLYE--NITDEEIYKS----LENVYLLDFVNQVgLDyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:cd03269    88 IDQLVYLAQlkGLKKEEARRRidewLERLELSEYANKR-VE--------ELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 498 LDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQG 547
Cdd:cd03269   159 LDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
346-547 1.16e-15

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 77.12  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLL----YPLKGNIFIQGKnydDLAEKSIRE---HFAVAFQEHHI 418
Cdd:PRK13548   15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALsgelSPDSGEVRLNGR---PLADWSPAElarRRAVLPQHSSL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 -FNLSIRDNFKM-LY----ENITDEEIykslenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA------KQK 486
Cdd:PRK13548   88 sFPFTVEEVVAMgRAphglSRAEDDAL--------VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 487 DIILLDEPTAGLDIK---TTNNICSQLMEKyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:PRK13548  160 RWLLLDEPTSALDLAhqhHVLRLARQLAHE-RGLAVIVVLHDLNLaARYADRIVLLHQGRLVADG 223
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
345-524 1.30e-15

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: 79.85  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM----------RLLY-----PLKGNIFIQGK-------------- 395
Cdd:TIGR03269  12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgRIIYhvalcEKCGYVERPSKvgepcpvcggtlep 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 396 ------NYDDLAEKSIREHFAVAFQEhhIFNLSIRDNfkmLYENITD--EEI-YKSLENVYL-LDFVNQVGLDYIVGNDG 465
Cdd:TIGR03269  92 eevdfwNLSDKLRRRIRKRIAIMLQR--TFALYGDDT---VLDNVLEalEEIgYEGKEAVGRaVDLIEMVQLSHRITHIA 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 466 NKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSH 524
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSH 227
PTZ00243 PTZ00243
ABC transporter; Provisional
346-543 1.43e-15

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 80.59  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddLAEKSIrehfAVAFQEHHIFNLSIRD 425
Cdd:PTZ00243   673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI----AYVPQQAWIMNATVRG 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  426 NFKMLyenitDEEIYKSLENVY----LLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PTZ00243   740 NILFF-----DEEDAARLADAVrvsqLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2674892663  500 IKTTNNICSQ-LMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKI 543
Cdd:PTZ00243   815 AHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
345-553 1.64e-15

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 76.28  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA--EKSIREHFAVAFQEHHIF-NL 421
Cdd:PRK09493   13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvdERLIRQEAGMVFQQFYLFpHL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNfkMLYENITDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-- 499
Cdd:PRK09493   93 TALEN--VMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpe 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 -----IKTTNNICSQLMekyqkqTMIVTSHDI-------SLLRFFDdiiiCGeeKIIEQGNIKKLL 553
Cdd:PRK09493  171 lrhevLKVMQDLAEEGM------TMVIVTHEIgfaekvaSRLIFID----KG--RIAEDGDPQVLI 224
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
331-525 1.88e-15

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 75.21  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDlaygydKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDL-AEksiR 406
Cdd:COG4136     5 ENLTITLGG------RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALpAE---Q 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHHIF-NLSIRDNFKM-LYENITDEE----IYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAI 480
Cdd:COG4136    76 RRIGILFQDDLLFpHLSVGENLAFaLPPTIGRAQrrarVEQALE---------EAGLAGFADRDPATLSGGQRARVALLR 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ---TMIVTsHD 525
Cdd:COG4136   147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRgipALLVT-HD 193
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
347-530 1.95e-15

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: 75.93  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQehhifnls 422
Cdd:COG4181    26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQ-------- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 irdNFkMLYENITdeeiykSLENVYL--------------LDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG4181    98 ---SF-QLLPTLT------ALENVMLplelagrrdararaRALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLR 530
Cdd:COG4181   168 LFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAA 211
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
345-557 2.23e-15

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 76.34  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQEHHIF-N 420
Cdd:PRK11831   19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALFtD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN--FKMLYENITDEEIYKSLENVYLldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK11831   99 MNVFDNvaYPLREHTQLPAPLLHSTVMMKL----EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 499 DiKTTNNICSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:PRK11831  175 D-PITMGVLVKLISELNSAlgvTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
349-547 2.46e-15

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: 78.96  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQE--------- 415
Cdd:COG4172   302 VDGVSLTLRRG-ETLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfgslsprm 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 ------------HHIfNLSIRDnfkmlyeniTDEEIYKSLEnvylldfvnQVGLDyivGNDGNK----LSGGQKHRLQLA 479
Cdd:COG4172   380 tvgqiiaeglrvHGP-GLSAAE---------RRARVAEALE---------EVGLD---PAARHRypheFSGGQRQRIAIA 437
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:COG4172   438 RALILEPKLLVLDEPTSALDVSVQAQIL-DLLRDLQREhglAYLFISHDLAVVRALaHRVMVMKDGKVVEQG 508
cbiO PRK13649
energy-coupling factor transporter ATPase;
349-524 2.75e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 76.32  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFI-------QGKNYDDlaeKSIREHFAVAFQ--EHHIF 419
Cdd:PRK13649   23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitsTSKNKDI---KQIRKKVGLVFQfpESQLF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKMLYEN--ITDEEIYK-SLENVYLldfvnqVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13649  100 EETVLKDVAFGPQNfgVSQEEAEAlAREKLAL------VGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNnicsQLMEKYQK-----QTMIVTSH 524
Cdd:PRK13649  174 AGLDPKGRK----ELMTLFKKlhqsgMTIVLVTH 203
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
330-547 4.04e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 76.43  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGYDK------VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ----GKNYDD 399
Cdd:PRK13631   17 SDDIILRVKNLYCVFDEkqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE------------KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKsLENVYLldfvNQVGLDY-IVG 462
Cdd:PRK13631   97 HELitnpyskkiknfKELRRRVSMVFQfpEYQLFKDTIEKDimFGPVALGVKKSEAKK-LAKFYL----NKMGLDDsYLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 463 NDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDI-SLLRFFDDIIICGE 540
Cdd:PRK13631  172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMeHVLEVADEVIVMDK 251

                  ....*..
gi 2674892663 541 EKIIEQG 547
Cdd:PRK13631  252 GKILKTG 258
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
4-493 4.89e-15

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 77.92  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663   4 ILSNMIRPVVWSLLLAILVGTISTLSSISLMGL-SAWLIASAALQPPLYVLSLAIVGVRFcgVMRAVFRYLERYFTHKVG 82
Cdd:COG4615     3 LLRLLLRESRWLLLLALLLGLLSGLANAGLIALiNQALNATGAALARLLLLFAGLLVLLL--LSRLASQLLLTRLGQHAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  83 FSLftsfRVFVLIKIIKAlPFKQQTENGDA--FDLIVNAVDNLRDSFlrFFLPPIITTISVFILSiwfFLYsydLMILli 160
Cdd:COG4615    81 ARL----RLRLSRRILAA-PLERLERIGAArlLAALTEDVRTISQAF--VRLPELLQSVALVLGC---LAY---LAWL-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 161 sSWLIFMIVIPYMI------WRRYLKLKKHKFLLTQEIIEFY-------EGNRELSFyNYDK---YRLKNINHSIEQYQQ 224
Cdd:COG4615   146 -SPPLFLLTLVLLGlgvagyRLLVRRARRHLRRAREAEDRLFkhfrallEGFKELKL-NRRRrraFFDEDLQPTAERYRD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 225 YQQNLFKLKLKVNLCSEFIMgaYLVICLAISIYLVNTQDFNPIMA-ITIILTY--QAVLEVLAMMPSLIEhFDEASKRWQ 301
Cdd:COG4615   224 LRIRADTIFALANNWGNLLF--FALIGLILFLLPALGWADPAVLSgFVLVLLFlrGPLSQLVGALPTLSR-ANVALRKIE 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 302 DLaifmqEKKFiaNTNNEIKSENQEDKQSKDVQLL-LKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKST 374
Cdd:COG4615   301 EL-----ELAL--AAAEPAAADAAAPPAPADFQTLeLRGVTYRYPGEDgdegftLGPIDLTIRRGELVFIVGGNGSGKST 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 375 LFYVLMRLLYPLKGNIFIQGK-----NYDDLaeksiREHFAVAFQEHHIFnlsirDNFKMLYENITDEEIYKSLEnvyll 449
Cdd:COG4615   374 LAKLLTGLYRPESGEILLDGQpvtadNREAY-----RQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLE----- 438
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 2674892663 450 dfvnQVGLDYIVGNDGNK-----LSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG4615   439 ----RLELDHKVSVEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
349-506 5.84e-15

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 76.38  E-value: 5.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQehHiFNL-SIR 424
Cdd:PRK11153   21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQ--H-FNLlSSR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 ---DN--FKMLYENITDEEIYKSLENvyLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK11153   98 tvfDNvaLPLELAGTPKAEIKARVTE--LLELV---GLsdkaDRYPAQ----LSGGQKQRVAIARALASNPKVLLCDEAT 168
                         170
                  ....*....|.
gi 2674892663 496 AGLDIKTTNNI 506
Cdd:PRK11153  169 SALDPATTRSI 179
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
345-524 6.92e-15

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 73.33  E-value: 6.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLY-PLKGNIFIQGKnydDLAEKSIREHFA----VAFQEhhi 418
Cdd:cd03217    12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYeVTEGEILFKGE---DITDLPPEERARlgifLAFQY--- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 fnlsirdnfkmlyenitDEEIykslENVYLLDFVNQVgldyivgNDGnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:cd03217    86 -----------------PPEI----PGVKNADFLRYV-------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
                         170       180
                  ....*....|....*....|....*..
gi 2674892663 499 DIKTTNNICSQLME-KYQKQTMIVTSH 524
Cdd:cd03217   136 DIDALRLVAEVINKlREEGKSVLIITH 162
cbiO PRK13650
energy-coupling factor transporter ATPase;
337-561 7.01e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 75.15  E-value: 7.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyDDLAEKS---IREHF 409
Cdd:PRK13650    7 VKNLTFKYKedqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENvwdIRHKI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYK----SLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAIC 481
Cdd:PRK13650   84 GMVFQnpDNQFVGATVEDDVAFGLENkgIPHEEMKErvneALELVGMQDFKER---------EPARLSGGQKQRVAIAGA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLD-------IKTTNNIcsqlMEKYQkQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:PRK13650  155 VAMRPKIIILDEATSMLDpegrlelIKTIKGI----RDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229

                  ....*..
gi 2674892663 555 REDSYLN 561
Cdd:PRK13650  230 RGNDLLQ 236
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
345-502 7.23e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 73.75  E-value: 7.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaekSIREhfAVAFQEHHIF---NL 421
Cdd:PRK13539   14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP---DVAE--ACHYLGHRNAmkpAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13539   89 TVAENleFWAAFLGGEELDIAAALE---------AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159

                  ...
gi 2674892663 500 IKT 502
Cdd:PRK13539  160 AAA 162
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
348-549 7.62e-15

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 75.95  E-value: 7.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMR----LLYPLKGNIFIQGKNYDdlAEKSIRE-HFAVAFQEHHIF-NL 421
Cdd:COG1118    17 LLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGRDLF--TNLPPRErRVGFVFQHYALFpHM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLENvyLLDFVNQVGLD--YIvgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:COG1118    91 TVAENiaFGLRVRPPSKAEIRARVEE--LLELVQLEGLAdrYP-----SQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 498 LDIKTTNNICSQLME---KYQKQTMIVTsHDISL-LRFFDDIIicgeekIIEQGNI 549
Cdd:COG1118   164 LDAKVRKELRRWLRRlhdELGGTTVFVT-HDQEEaLELADRVV------VMNQGRI 212
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
346-526 1.16e-14

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 74.35  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---------------------S 404
Cdd:COG1101    19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakyigrvfqdpmmgtapsmT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 405 IREHFAVAFQEHHIFNLSIRDNFKmlyenitDEEIYKS--------LENvyLLDfvNQVGLdyivgndgnkLSGGQKHRL 476
Cdd:COG1101    99 IEENLALAYRRGKRRGLRRGLTKK-------RRELFREllatlglgLEN--RLD--TKVGL----------LSGGQRQAL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 477 QLAICLAKQKDIILLDEPTAGLDIKTTNNI---CSQLMEKYQKQTMIVTsHDI 526
Cdd:COG1101   158 SLLMATLTKPKLLLLDEHTAALDPKTAALVlelTEKIVEENNLTTLMVT-HNM 209
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
349-530 1.36e-14

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: 73.92  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEksirehFAVA-------FQEHHIF-N 420
Cdd:COG0411    20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP------HRIArlgiartFQNPRLFpE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENITDEEIYKSLENV---------------YLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAIC 481
Cdd:COG0411    94 LTVLENVLVAAHARLGRGLLAALLRLprarreereareraeELLERV---GLadraDEPAGN----LSYGQQRRLEIARA 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLR 530
Cdd:COG0411   167 LATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVM 217
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
337-547 1.67e-14

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 75.65  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:PRK09536    6 VSDLSVEFgDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI-FNLSIRDNFKM---------LYENITDEEIYKSLenvylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK09536   86 TSLsFEFDVRQVVEMgrtphrsrfDTWTETDRAAVERA--------MERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 486 KDIILLDEPTAGLDIK---TTNNICSQLMEkyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:PRK09536  158 TPVLLLDEPTASLDINhqvRTLELVRRLVD--DGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
348-547 1.84e-14

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: 72.30  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIR 424
Cdd:cd03233    22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DnfkmlyenitdeeiykslenvyLLDFVNQV-GLDYIVGndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTT 503
Cdd:cd03233   102 E----------------------TLDFALRCkGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 504 NNI--CSQLMEKYQKQTMIVT----SHDISLLrfFDDIIICGEEKIIEQG 547
Cdd:cd03233   155 LEIlkCIRTMADVLKTTTFVSlyqaSDEIYDL--FDKVLVLYEGRQIYYG 202
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
351-547 2.00e-14

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 74.38  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQE-HHIFN--LSI 423
Cdd:COG4608    36 GVSFDIRRG-ETLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpYASLNprMTV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RD-------NFKMLYENITDEEIYKSLEnvylldfvnQVGLDyivGNDGNK----LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG4608   115 GDiiaeplrIHGLASKAERRERVAELLE---------LVGLR---PEHADRypheFSGGQRQRIGIARALALNPKLIVCD 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 493 EPTAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQG 547
Cdd:COG4608   183 EPVSALDV----SIQAQvlnLLEDLQDElglTYLFISHDLSVVRHIsDRVAVmyLG--KIVEIA 240
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
337-553 2.87e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 73.15  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLKGNIFIQGKNY---DDLAEKSI-----RE 407
Cdd:PRK14258   10 VNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEffnQNIYERRVnlnrlRR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQEHHIFNLSIRDNFKMLYENI-------TDEEIYKSLENVYLLDFVNQVgldyiVGNDGNKLSGGQKHRLQLAI 480
Cdd:PRK14258   89 QVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleIDDIVESALKDADLWDEIKHK-----IHKSALDLSGGQQQRLCIAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICS--QLMEKYQKQTMIVTSHD---ISLLRFFDDIIICGEEKI---IEQGNIKKL 552
Cdd:PRK14258  164 ALAVKPKVLLMDEPCFGLDPIASMKVESliQSLRLRSELTMVIVSHNlhqVSRLSDFTAFFKGNENRIgqlVEFGLTKKI 243

                  .
gi 2674892663 553 L 553
Cdd:PRK14258  244 F 244
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
329-549 3.15e-14

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: 72.18  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 329 QSKDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAeksireh 408
Cdd:cd03220    18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEhhifNLSIRDN--FKMLYENITDEEIYKSLENVY----LLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICL 482
Cdd:cd03220    91 LGGGFNP----ELTGRENiyLNGRLLGLSRKEIDEKIDEIIefseLGDF-----IDLPVKT----YSSGMKARLAFAIAT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNiCSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:cd03220   158 ALEPDILLIDEVLAVGDAAFQEK-CQRRLRELLKQgkTVILVSHDPSSIKRLCDRAL-----VLEKGKI 220
cbiO PRK13643
energy-coupling factor transporter ATPase;
349-549 3.46e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 73.23  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE----KSIREHFAVAFQ--EHHIFNLS 422
Cdd:PRK13643   22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQfpESQLFEET 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYEN--ITDEEIYKslenvYLLDFVNQVGLDYIVGNDGN-KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13643  102 VLKDVAFGPQNfgIPKEKAEK-----IAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 500 IKTTNNICSQLMEKYQK-QTMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:PRK13643  177 PKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVY-----LLEKGHI 222
PTZ00243 PTZ00243
ABC transporter; Provisional
347-564 3.85e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 75.97  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDN 426
Cdd:PTZ00243  1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  427 FKMLYEnITDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ-KDIILLDEPTAGLDIKTT 503
Cdd:PTZ00243  1404 VDPFLE-ASSAEVWAALELVGLRERVasESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALD 1482
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663  504 NNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLI 564
Cdd:PTZ00243  1483 RQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
335-525 4.40e-14

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 74.10  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAE-KSIREHFAVA 412
Cdd:PRK11607   20 LEIRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV---DLSHvPPYQRPINMM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11607   97 FQSYALFpHMTVEQNiaFGLKQDKLPKAEIASRVNEMLGL-----VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQK--QTMIVTSHD 525
Cdd:PRK11607  172 LLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHD 209
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
352-551 4.97e-14

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: 74.84  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLAEKSI------REHFAVAFQEHHIF-NLSI 423
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdgrgraKRYIGILHQEYDLYpHRTV 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNfkmLYENITDE---EIYKsLENVYLLdfvNQVGLD-----YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR03269 383 LDN---LTEAIGLElpdELAR-MKAVITL---KMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQK--QTMIVTSHDISLLRffddiIICGEEKIIEQGNIKK 551
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVL-----DVCDRAALMRDGKIVK 508
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
321-525 5.59e-14

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 73.83  E-value: 5.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKDVQLLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD 399
Cdd:PRK09452    1 SKKLNKQPSSLSPLVELRGISKSFDgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 L-AEKsirEHFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIYK----SLENVYLLDFVNQVGLDyivgndgnkLSGG 471
Cdd:PRK09452   81 VpAEN---RHVNTVFQSYALFpHMTVFENvaFGLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPHQ---------LSGG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLmEKYQKQ---TMIVTSHD 525
Cdd:PRK09452  149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHD 204
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
319-540 6.52e-14

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: 75.33  E-value: 6.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  319 EIKSENQEDKQSK-DVQLLLKDLAYgYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKny 397
Cdd:TIGR01271  412 KIKQNNKARKQPNgDDGLFFSNFSL-YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-- 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  398 ddlaeksirehFAVAFQEHHIFNLSIRDN--FKMLYenitDEEIYKSLENVYLLD-----FVNQvglDYIV-GNDGNKLS 469
Cdd:TIGR01271  489 -----------ISFSPQTSWIMPGTIKDNiiFGLSY----DEYRYTSVIKACQLEedialFPEK---DKTVlGEGGITLS 550
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663  470 GGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEK-YQKQTMIVTSHDISLLRFFDDIIICGE 540
Cdd:TIGR01271  551 GGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKlMSNKTRILVTSKLEHLKKADKILLLHE 622
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
341-529 9.22e-14

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 70.67  E-value: 9.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEHH 417
Cdd:PRK10908   10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQDHH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IF-NLSIRDNFKM--LYENITDEEIYK----SLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK10908   90 LLmDRTVYDNVAIplIIAGASGDDIRRrvsaALDKVGLLDKAKNFPI---------QLSGGEQQRVGIARAVVNKPAVLL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2674892663 491 LDEPTAGLDIKTTNNICsQLMEKYQK--QTMIVTSHDISLL 529
Cdd:PRK10908  161 ADEPTGNLDDALSEGIL-RLFEEFNRvgVTVLMATHDIGLI 200
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
319-569 1.19e-13

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: 71.43  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 319 EIKSENQEDK-QSKDVQLLLKDLAYgYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKny 397
Cdd:cd03291    23 KAKQENNDRKhSSDDNNLFFSNLCL-VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 ddlaeksirehFAVAFQEHHIFNLSIRDN--FKMLYenitDEEIYKSLENVYLL--DFVNQVGLDYIV-GNDGNKLSGGQ 472
Cdd:cd03291   100 -----------ISFSSQFSWIMPGTIKENiiFGVSY----DEYRYKSVVKACQLeeDITKFPEKDNTVlGEGGITLSGGQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQ-KQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKK 551
Cdd:cd03291   165 RARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMaNKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSE 244
                         250
                  ....*....|....*...
gi 2674892663 552 LLLREDSYLNKLIRYKNF 569
Cdd:cd03291   245 LQSLRPDFSSKLMGYDTF 262
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
355-537 1.64e-13

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 70.51  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 355 SIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddlaeksirehfaVAFQEHHI---FNLSIRDnfkMLY 431
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------------VSYKPQYIkadYEGTVRD---LLS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 432 ENITDeeiyKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT---TNNICS 508
Cdd:cd03237    84 SITKD----FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIR 159
                         170       180
                  ....*....|....*....|....*....
gi 2674892663 509 QLMEKYQKqTMIVTSHDISLLRFFDDIII 537
Cdd:cd03237   160 RFAENNEK-TAFVVEHDIIMIDYLADRLI 187
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
335-549 1.76e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 70.31  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVA 412
Cdd:PRK10895    4 LTAKNLAKAYKgRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDNFKMLYEniTDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK10895   84 PQEASIFRrLSVYDNLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNIcSQLMEKYQKQTM--IVTSHDISllrffDDIIICGEEKIIEQGNI 549
Cdd:PRK10895  162 DEPFAGVDPISVIDI-KRIIEHLRDSGLgvLITDHNVR-----ETLAVCERAYIVSQGHL 215
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
335-549 2.30e-13

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 70.09  E-value: 2.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfIQGKNydDLAEksIREHFAVAF 413
Cdd:PRK11247   13 LLLNAVSKRYgERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA--PLAE--AREDTRLMF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHH-------IFN--LSIRDNFKmlyenitdEEIYKSLENVYLLDFVNqvglDYIVGndgnkLSGGQKHRLQLAICLAK 484
Cdd:PRK11247   88 QDARllpwkkvIDNvgLGLKGQWR--------DAALQALAAVGLADRAN----EWPAA-----LSGGQKQRVALARALIH 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:PRK11247  151 RPGLLLLDEPLGALDALTRIEM-QDLIESLWQQhgfTVLLVTHDVSEAVAMADRVL-----LIEEGKI 212
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
346-545 2.92e-13

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 70.10  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREHFAVAFQE------- 415
Cdd:PRK10419   25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsisavnp 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENITDEEIYKSLEnvyLLDfvnQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK10419  105 RKTVREIIREPLRHLLSLDKAERLARASE---MLR---AVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLmEKYQKQT---MIVTSHDISLL-RFFDDIIICGEEKIIE 545
Cdd:PRK10419  179 VSNLDLVLQAGVIRLL-KKLQQQFgtaCLFITHDLRLVeRFCQRVMVMDNGQIVE 232
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
349-530 2.95e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 72.12  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK-SIREHFAVAFQEHHIFN-LSIRDN 426
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDeLTVLEN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F--------KMLYENITDEEIYKSLENVYLLDFVNQVGLDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK09700  101 LyigrhltkKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 499 DIKTTNN---ICSQLmeKYQKQTMIVTSHDISLLR 530
Cdd:PRK09700  177 TNKEVDYlflIMNQL--RKEGTAIVYISHKLAEIR 209
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
337-525 3.13e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 72.29  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehFAVAFQE 415
Cdd:PRK11147  322 MENVNYQIdGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------------LEVAYFD 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNL----SIRDNfkmLYENITDEEIYKSLENV--YLLDFV-------NQVgldyivgndgNKLSGGQKHRLQLAICL 482
Cdd:PRK11147  389 QHRAELdpekTVMDN---LAEGKQEVMVNGRPRHVlgYLQDFLfhpkramTPV----------KALSGGERNRLLLARLF 455
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTnNICSQLMEKYQKQTMIVtSHD 525
Cdd:PRK11147  456 LKPSNLLILDEPTNDLDVETL-ELLEELLDSYQGTVLLV-SHD 496
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
339-497 5.08e-13

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: 68.71  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSiREHFAVAF--QEH 416
Cdd:TIGR03410   7 NVYYGQSHIL-RGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIAYvpQGR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF-NLSIRDNFKMLYENITD------EEIYkSLENVyLLDFVNQVGldyivgndGNkLSGGQkhRLQLAI--CLAKQKD 487
Cdd:TIGR03410  85 EIFpRLTVEENLLTGLAALPRrsrkipDEIY-ELFPV-LKEMLGRRG--------GD-LSGGQ--QQQLAIarALVTRPK 151
                         170
                  ....*....|
gi 2674892663 488 IILLDEPTAG 497
Cdd:TIGR03410 152 LLLLDEPTEG 161
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
349-526 9.11e-13

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 68.74  E-value: 9.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKsirehfAVAFQEHHIFN-LSIRDN 426
Cdd:COG4525    23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgADR------GVVFQKDALLPwLNVLDN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --FKMLYENITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:COG4525    97 vaFGLRLRGVPKAERRARAE-----ELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
                         170       180
                  ....*....|....*....|....*
gi 2674892663 505 NICSQLMEKYQ---KQTMIVTsHDI 526
Cdd:COG4525   172 QMQELLLDVWQrtgKGVFLIT-HSV 195
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
339-553 9.64e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 68.58  E-value: 9.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-----YPLKGNIFIQGK---NYDDLAEksIREHF 409
Cdd:PRK14271   26 NLTLGFaGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRsifNYRDVLE--FRRRV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFNLSIRDNF--KMLYENITDEEIYKSLENVYLldfvNQVGL-DYI---VGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK14271  104 GMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQARL----TEVGLwDAVkdrLSDSPFRLSGGQQQLLCLARTLA 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK14271  180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
346-528 1.00e-12

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: 67.13  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRD 425
Cdd:cd03231    13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKMLYENITDEEIYKSLENVYLLDFVnqvglDYIVgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:cd03231    93 NLRFWHADHSDEQVEEALARVGLNGFE-----DRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
                         170       180
                  ....*....|....*....|...
gi 2674892663 506 ICSQLMEKYQKQTMIVTSHDISL 528
Cdd:cd03231   164 FAEAMAGHCARGGMVVLTTHQDL 186
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
325-539 1.08e-12

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 67.68  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVQLLLKDLAYGYDKV---LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLY--PLKGNIFIQGKNYDD 399
Cdd:COG2401    19 SVLDLSERVAIVLEAFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 laEKSIREHFAvafqehhifnlsIRDNFKmlyenitdeeiykslENVYLLdfvNQVGLdyivgNDG-------NKLSGGQ 472
Cdd:COG2401    99 --EASLIDAIG------------RKGDFK---------------DAVELL---NAVGL-----SDAvlwlrrfKELSTGQ 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLDiKTTNNICSQLMEKYQKQ---TMIVTSHDISLLRFF--DDIIICG 539
Cdd:COG2401   142 KFRFRLALLLAERPKLLVIDEFCSHLD-RQTAKRVARNLQKLARRagiTLVVATHHYDVIDDLqpDLLIFVG 212
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
349-541 1.15e-12

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 68.41  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvLMRLLYP-LKGNIFIQGKNYDDLAEKSIREH------------------- 408
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSL---INDTLYPaLARRLHLKKEQPGNHDRIEGLEHidkvividqspigrtprsn 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 ---FAVAFQEhhifnlsIRDNF--------------KMLYE--NITD------EEIYKSLENV----YLLDFVNQVGLDY 459
Cdd:cd03271    88 patYTGVFDE-------IRELFcevckgkrynretlEVRYKgkSIADvldmtvEEALEFFENIpkiaRKLQTLCDVGLGY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 460 I-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPTAGL---DIKTTNNICSQLMEKyqKQTMIVTSHDISLLRFF 532
Cdd:cd03271   161 IkLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK--GNTVVVIEHNLDVIKCA 238

                  ....*....
gi 2674892663 533 DDIIICGEE 541
Cdd:cd03271   239 DWIIDLGPE 247
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
357-538 1.15e-12

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: 68.16  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNiFIQGKNYDDLaeksIREHFAVAFQEH--HIFNLSIRDNFKMLYENI 434
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI----LDEFRGSELQNYftKLLEGDVKVIVKPQYVDL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 435 --------TDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:cd03236    99 ipkavkgkVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2674892663 507 CSQLMEKYQ-KQTMIVTSHDISLLRFFDDIIIC 538
Cdd:cd03236   179 ARLIRELAEdDNYVLVVEHDLAVLDYLSDYIHC 211
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
334-499 1.24e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 70.39  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV 411
Cdd:PRK10522  322 TLELRNVTFAYQDngFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFN-LSIRDNFKmlyeniTDEEIYKS-LENvylLDFVNQVGLDyivgnDGN----KLSGGQKHRLQLAICLAKQ 485
Cdd:PRK10522  402 VFTDFHLFDqLLGPEGKP------ANPALVEKwLER---LKMAHKLELE-----DGRisnlKLSKGQKKRLALLLALAEE 467
                         170
                  ....*....|....
gi 2674892663 486 KDIILLDEPTAGLD 499
Cdd:PRK10522  468 RDILLLDEWAADQD 481
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
349-512 2.44e-12

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: 65.53  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREHFA--VAF-----QEHHIF-N 420
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK---PVTRRSPRDAIRagIAYvpedrKREGLVlD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMlyenitdeeiykslenvylldfvnqvgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:cd03215    93 LSVAENIAL-----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
                         170
                  ....*....|..
gi 2674892663 501 KTTNNICSQLME 512
Cdd:cd03215   138 GAKAEIYRLIRE 149
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
349-526 2.50e-12

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 67.03  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKsirehfAVAFQEHHIFN-LSIRDN 426
Cdd:PRK11248   17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgAER------GVVFQNEGLLPwRNVQDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --FKMLYENITDEEiykslENVYLLDFVNQVGLD-----YIVgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK11248   91 vaFGLQLAGVEKMQ-----RLEIAHQMLKKVGLEgaekrYIW-----QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 2674892663 500 IKTTNNICSQLMEKYQ---KQTMIVTsHDI 526
Cdd:PRK11248  161 AFTREQMQTLLLKLWQetgKQVLLIT-HDI 189
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
349-553 3.32e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 67.80  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN-YDDlaEKSIREHFAVAF-QEHH-IFNLSIRD 425
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKR--RKEFARRIGVVFgQRSQlWWDLPAID 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKML---YEnITDEEIYKSLENvylldFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:COG4586   116 SFRLLkaiYR-IPDAEYKKRLDE-----LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 503 TNNIcSQLMEKYQKQ---TMIVTSHDIsllrffDDI-------IICGEEKIIEQGNIKKLL 553
Cdd:COG4586   190 KEAI-REFLKEYNRErgtTILLTSHDM------DDIealcdrvIVIDHGRIIYDGSLEELK 243
cbiO PRK13642
energy-coupling factor transporter ATPase;
335-553 4.10e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 67.04  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV----LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:PRK13642    5 LEVENLVFKYEKEsdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLEN----VYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICL 482
Cdd:PRK13642   85 MVFQnpDNQFVGATVEDDvaFGMENQGIPREEMIKRVDEallaVNMLDFKTR---------EPARLSGGQKQRVAVAGII 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13642  156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSitHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
PLN03130 PLN03130
ABC transporter C family member; Provisional
239-552 4.17e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 69.38  E-value: 4.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  239 CSEFIMGA--YLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDEAS---KRWQDLaiFMQEKKFI 313
Cdd:PLN03130   525 FNSFILNSipVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANvslKRLEEL--LLAEERVL 602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  314 AnTNNEIKSENQedkqskdvQLLLKDLAYGYD----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGN 389
Cdd:PLN03130   603 L-PNPPLEPGLP--------AISIKNGYFSWDskaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA 673
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  390 IFIqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNfkMLYENITDEEIYKSLENVYLLdfvnQVGLDYIVGND----- 464
Cdd:PLN03130   674 SVV------------IRGTVAYVPQVSWIFNATVRDN--ILFGSPFDPERYERAIDVTAL----QHDLDLLPGGDlteig 735
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  465 --GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQ-LMEKYQKQTMIVTSHDISLLRFFDDIIICGEE 541
Cdd:PLN03130   736 erGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEG 815
                          330
                   ....*....|.
gi 2674892663  542 KIIEQGNIKKL 552
Cdd:PLN03130   816 MIKEEGTYEEL 826
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
335-524 5.82e-12

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: 65.07  E-value: 5.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREHFAVAF 413
Cdd:TIGR01189   1 LAARNLACSRGeRMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---PLAEQRDEPHENILY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHH--IFN-LSIRDNFKMLYENITDEE--IYKSLENVYLLDFVnqvglDYIVgndgNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR01189  78 LGHLpgLKPeLSALENLHFWAAIHGGAQrtIEDALAAVGLTGFE-----DLPA----AQLSAGQQRRLALARLWLSRRPL 148
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIV-TSH 524
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLlTTH 185
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
342-525 8.57e-12

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 66.65  E-value: 8.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE-HFAVAFQEHHIF- 419
Cdd:PRK10851   12 FGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARDrKVGFVFQHYALFr 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN----FKML--YENITDEEIYKSLenVYLLDFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:PRK10851   88 HMTVFDNiafgLTVLprRERPNAAAIKAKV--TQLLEMVQ---LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 494 PTAGLDIKTTNNI---CSQLMEKYQKQTMIVTsHD 525
Cdd:PRK10851  163 PFGALDAQVRKELrrwLRQLHEELKFTSVFVT-HD 196
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
338-537 9.44e-12

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: 64.19  E-value: 9.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAY-----GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQGKNYDDLAEKSIrehfa 410
Cdd:cd03232     7 KNLNYtvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKNFQRST----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 vAFQEH---HIFNLSIRDnfkmlyenitdeeiykSLENVYLLdfvnqvgldyivgndgNKLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03232    82 -GYVEQqdvHSPNLTVRE----------------ALRFSALL----------------RGLSVEQRKRLTIGVELAAKPS 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 488 IILLDEPTAGLDIKTTNNICsQLMEKY--QKQTMIVTSH--DISLLRFFDDIII 537
Cdd:cd03232   129 ILFLDEPTSGLDSQAAYNIV-RFLKKLadSGQAILCTIHqpSASIFEKFDRLLL 181
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
349-534 1.26e-11

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


Pssm-ID: 443710 [Multi-domain]  Cd Length: 250  Bit Score: 64.75  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSirEHfAVA-------FQEHHIF-N 420
Cdd:COG4674    26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT---DLTGLD--EH-EIArlgigrkFQKPTVFeE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN-----------FKMLYENITDEE---IYKSLENVYLLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICLAKQK 486
Cdd:COG4674   100 LTVFENlelalkgdrgvFASLFARLTAEErdrIEEVLETIGLTDK-----ADRLAGL----LSHGQKQWLEIGMLLAQDP 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDD 534
Cdd:COG4674   171 KLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIAR 218
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
346-547 1.46e-11

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 67.04  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEKS---IREHFAVAFQEHhifNLS 422
Cdd:PRK15134  299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDP---NSS 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IrdNFKMLYENITDEEI---YKSL----ENVYLLDFVNQVGLD------YivgndGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK15134  375 L--NPRLNVLQIIEEGLrvhQPTLsaaqREQQVIAVMEEVGLDpetrhrY-----PAEFSGGQRQRIAIARALILKPSLI 447
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:PRK15134  448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALcHQVIVLRQGEVVEQG 508
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
349-550 1.46e-11

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 64.72  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddLAekSIREhFAVAFQEhhifNLSIRDN-- 426
Cdd:COG1134    42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VS--ALLE-LGAGFHP----ELTGRENiy 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMLYENITDEEIYKSLENVylLDFVnQVGlDYI---VGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI--- 500
Cdd:COG1134   111 LNGRLLGLSRKEIDEKFDEI--VEFA-ELG-DFIdqpVKT----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafq 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 501 -KttnniCSQLMEKYQKQ--TMIVTSHDISLLR-FFDDIIicgeekIIEQGNIK 550
Cdd:COG1134   183 kK-----CLARIRELRESgrTVIFVSHSMGAVRrLCDRAI------WLEKGRLV 225
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
352-549 1.49e-11

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: 67.73  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEkSIREHFAVAFQEHHIFN-LSIRDNFkML 430
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLD-AVRQSLGMCPQHNILFHhLTVAEHI-LF 1026
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  431 YENI---TDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC 507
Cdd:TIGR01257 1027 YAQLkgrSWEEAQLEMEAM-----LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2674892663  508 SQLMEKYQKQTMIVTSHDISLLRFFDDIIicgeeKIIEQGNI 549
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLLGDRI-----AIISQGRL 1138
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
338-536 2.27e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 66.50  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMrllyplkgnifiqGKNYDDLAEKSIREHFAVAFQEH 416
Cdd:TIGR03719 326 ENLTKAFgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT-------------GQEQPDSGTIEIGETVKLAYVDQ 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLsirDNFKMLYENITDeeiykslenvylldfvnqvGLDYIV------------------GNDGNK----LSGGQKH 474
Cdd:TIGR03719 393 SRDAL---DPNKTVWEEISG-------------------GLDIIKlgkreipsrayvgrfnfkGSDQQKkvgqLSGGERN 450
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHDisllRFFDDII 536
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHD----RWFLDRI 506
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
351-553 4.15e-11

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 65.50  E-value: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL------YPlKGNIFIQGKNYDDLAEKSIR----EHFAVAFQEHHIFN 420
Cdd:PRK15134   27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvvYP-SGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMVSL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENIT----------DEEIYKSLENV-------YLLDFVNQvgldyivgndgnkLSGGQKHRLQLAICLA 483
Cdd:PRK15134  106 NPLHTLEKQLYEVLSlhrgmrreaaRGEILNCLDRVgirqaakRLTDYPHQ-------------LSGGERQRVMIAMALL 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK15134  173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRkLADRVAVMQNGRCVEQNRAATLF 245
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
338-533 4.34e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 65.90  E-value: 4.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  338 KDLAY-----GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKNYDDLAEKSIRehf 409
Cdd:TIGR00956  763 RNLTYevkikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSSFQRSIG--- 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  410 AVAFQEHHIFNLSIRDNFKM-----LYENITDEEIYKSLENVY-LLDFVNQVglDYIVGNDGNKLSGGQKHRLQLAICL- 482
Cdd:TIGR00956  840 YVQQQDLHLPTSTVRESLRFsaylrQPKSVSKSEKMEYVEEVIkLLEMESYA--DAVVGVPGEGLNVEQRKRLTIGVELv 917
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663  483 AKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQK--QTMIVTSHDISLLRF--FD 533
Cdd:TIGR00956  918 AKPKLLLFLDEPTSGLDSQTAWSIC-KLMRKLADhgQAILCTIHQPSAILFeeFD 971
ycf16 CHL00131
sulfate ABC transporter protein; Validated
345-549 5.21e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.12  E-value: 5.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRllYP----LKGNIFIQGKNYDDLaEKSIREHFAV--AFQEH-H 417
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDL-EPEERAHLGIflAFQYPiE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ----VGLD--YIVGNDGNKLSGGQKHR---LQLAICLAKqkdI 488
Cdd:CHL00131   96 IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEklklVGMDpsFLSRNVNEGFSGGEKKRneiLQMALLDSE---L 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 489 ILLDEPTAGLDI---KTTNNICSQLMEKyqKQTMIVTSHDISLLRFF--DDIIICGEEKIIEQGNI 549
Cdd:CHL00131  173 AILDETDSGLDIdalKIIAEGINKLMTS--ENSIILITHYQRLLDYIkpDYVHVMQNGKIIKTGDA 236
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
345-538 7.10e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 62.82  E-value: 7.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaEKSIREHFAVAFQEHHI---FNL 421
Cdd:PRK09544   16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLdttLPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRdNFKMLYENITDEEIYKSLENV---YLLDFVNQvgldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK09544   85 TVN-RFLRLRPGTKKEDILPALKRVqagHLIDAPMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2674892663 499 DIK---TTNNICSQLMEKYQKQTMIVtSHDISLLRFFDDIIIC 538
Cdd:PRK09544  152 DVNgqvALYDLIDQLRRELDCAVLMV-SHDLHLVMAKTDEVLC 193
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
339-530 7.47e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 61.89  E-value: 7.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD-DLAeksirehfavAFQEH 416
Cdd:PRK13540    6 ELDFDYhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLC----------TYQKQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF---------NLSIRDNfkMLYenitdeEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK13540   76 LCFvghrsginpYLTLREN--CLY------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSH-DISLLR 530
Cdd:PRK13540  148 LWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHqDLPLNK 192
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
325-553 1.21e-10

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 62.11  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVQLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK 403
Cdd:PRK10575    2 QEYTNHSDTTFALRNVSFRVpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 S-------------------IREHFAVAFQEHH--IFNLSIRDNFKMlyenitDEEIykslenvylldfvNQVGLDYIVG 462
Cdd:PRK10575   82 AfarkvaylpqqlpaaegmtVRELVAIGRYPWHgaLGRFGAADREKV------EEAI-------------SLVGLKPLAH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 463 NDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICS--QLMEKYQKQTMIVTSHDISL-LRFFDDIIICG 539
Cdd:PRK10575  143 RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAlvHRLSQERGLTVIAVLHDINMaARYCDYLVALR 222
                         250
                  ....*....|....
gi 2674892663 540 EEKIIEQGNIKKLL 553
Cdd:PRK10575  223 GGEMIAQGTPAELM 236
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
295-524 1.70e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 62.54  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 295 EASKRWQDLAIFMQEKKFIANTNNEIKSenqeDKQSKDVQLLLKDLAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKST 374
Cdd:PRK13536    8 EEAPRRLELSPIERKHQGISEAKASIPG----SMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 375 LFYVLMRLLYPLKGNIFIQGKNYDDLAeKSIREHFAVAFQEHHI-FNLSIRDN-------FKMLYENItdEEIYKSLenv 446
Cdd:PRK13536   83 IARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQFDNLdLEFTVRENllvfgryFGMSTREI--EAVIPSL--- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 447 ylLDFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSH 524
Cdd:PRK13536  157 --LEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTH 230
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
349-537 2.03e-10

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: 59.36  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehfAVAFqehhifnLSIRDnfk 428
Cdd:cd03216    16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------EVSF-------ASPRD--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 mlyenitdeeiykSLEN-VYLldfVNQvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC 507
Cdd:cd03216    72 -------------ARRAgIAM---VYQ-------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2674892663 508 sQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIII 537
Cdd:cd03216   123 -KVIRRLRAQgvAVIFISHRLDeVFEIADRVTV 154
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
349-553 2.06e-10

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 61.39  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvLMRL--LYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE---------HH 417
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqsppfampvFQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNfkmlyeniTDEEIYKSLenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLA-ICLakQKD--------I 488
Cdd:COG4138    89 YLALHQPAG--------ASSEAVEQL----LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAaVLL--QVWptinpegqL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDI---KTTNNICSQLMEkyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4138   155 LLLDEPMNSLDVaqqAALDRLLRELCQ--QGITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEVM 221
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
347-547 2.47e-10

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: 60.46  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAEK-SIREHFAVAFQEHHIFN-LSIR 424
Cdd:cd03266    19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaEARRRLGFVSDSTGLYDrLTAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DN---FKMLY----ENITD--EEIYKSLENVYLLDfvnqvgldyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03266    97 ENleyFAGLYglkgDELTArlEELADRLGMEELLD------------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNNICSQLME-KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03266   165 TGLDVMATRALREFIRQlRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
349-549 2.67e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 61.18  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---------YPLKGN-IFIQGKNYDDLaEKSiREHFAVAFQEHHI 418
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagshIELLGRtVQREGRLARDI-RKS-RANTGYIFQQFNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FN-LSIRDNfkMLYENITDEEIYKS-------LENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK09984   98 VNrLSVLEN--VLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDIIicgeekIIEQGNI 549
Cdd:PRK09984  176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIV------ALRQGHV 231
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
318-537 3.56e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 62.52  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 318 NEIKSENQEDKQSKDVQLLLK--DLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK 395
Cdd:PRK13409  322 EPIEFEERPPRDESERETLVEypDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 396 nyddlaeksirehfaVAFQEHHI---FNLSIRDNFKMLYENItDEEIYKSlenvyllDFVNQVGLDYIVGNDGNKLSGGQ 472
Cdd:PRK13409  402 ---------------ISYKPQYIkpdYDGTVEDLLRSITDDL-GSSYYKS-------EIIKPLQLERLLDKNVKDLSGGE 458
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLD----IKTTNNIcSQLMEKyQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PRK13409  459 LQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAI-RRIAEE-REATALVVDHDIYMIDYISDRLM 525
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
349-553 4.45e-10

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: 62.01  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLL-YP---LKGNIFIQGKNYDDLAEKSIRE----HFAVAFQE---- 415
Cdd:COG4172    26 VKGVSFDIAAG-ETLaLVGESGSGKSVTALSILRLLpDPaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpmts 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 ----HHIFN-----LsirdnfkMLYENITDEEI-YKSLEnvyLLDfvnQVGLDyivgNDGNK-------LSGGQKHRLQL 478
Cdd:COG4172   105 lnplHTIGKqiaevL-------RLHRGLSGAAArARALE---LLE---RVGIP----DPERRldayphqLSGGQRQRVMI 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQT---MIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4172   168 AMALANEPDLLIADEPTTALDVTVQAQIL-DLLKDLQRELgmaLLLITHDLGVVRrFADRVAVMRQGEIVEQGPTAELF 245
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
332-528 4.57e-10

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 59.79  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIR- 406
Cdd:PRK10584    8 EVHHLKKSVGQGEHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRa 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHhifnlsirdnfkMLYENITdeeiykSLENVYL----------------LDFVNQVGLDYIVGNDGNKLSG 470
Cdd:PRK10584   88 KHVGFVFQSF------------MLIPTLN------ALENVELpallrgessrqsrngaKALLEQLGLGKRLDHLPAQLSG 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDISL 528
Cdd:PRK10584  150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREHGTTLILVTHDLQL 209
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
364-547 4.80e-10

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: 61.36  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEI- 439
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENvaFGLKMRKVPRAEIk 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 440 ---YKSLENVYLLDFvnqvGLDYIvgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLmEKYQK 516
Cdd:TIGR01187  79 prvLEALRLVQLEEF----ADRKP-----HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL-KTIQE 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 517 Q---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR01187 149 QlgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIG 183
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
349-547 5.21e-10

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: 62.34  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYvlmRLLYPLKGNIFIQGK----NYDDL--AEK------------------- 403
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN---DTLYPALANRLNGAKtvpgRYTSIegLEHldkvihidqspigrtprsn 700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 ---------SIREHFA-------VAFQEHHI-FN--------------LSIRDNF-----------------------KM 429
Cdd:TIGR00630 701 patytgvfdEIRELFAetpeakvRGYTPGRFsFNvkggrceacqgdgvIKIEMHFlpdvyvpcevckgkrynretlevKY 780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 430 LYENITD------EEIYKSLENV----YLLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPT 495
Cdd:TIGR00630 781 KGKNIADvldmtvEEAYEFFEAVpsisRKLQTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT 860
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 496 AGL---DIKTTNNICSQLMEkyQKQTMIVTSHDISLLRFFDDIIICGEE------KIIEQG 547
Cdd:TIGR00630 861 TGLhfdDIKKLLEVLQRLVD--KGNTVVVIEHNLDVIKTADYIIDLGPEggdgggTVVASG 919
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
352-547 5.91e-10

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.00  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV-AFQEHHIF-NLSIRDN--- 426
Cdd:PRK11300   24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrTFQHVRLFrEMTVIENllv 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --------------FKM-LYENITDEEIYKS---LENVYLLDFVNQVGldyivgndGNkLSGGQKHRLQLAICLAKQKDI 488
Cdd:PRK11300  104 aqhqqlktglfsglLKTpAFRRAESEALDRAatwLERVGLLEHANRQA--------GN-LAYGQQRRLEIARCMVTQPEI 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 489 ILLDEPTAGLDIKTT---NNICSQLMEKYQkQTMIVTSHDISLLRFFDDIIIcgeekIIEQG 547
Cdd:PRK11300  175 LMLDEPAAGLNPKETkelDELIAELRNEHN-VTVLLIEHDMKLVMGISDRIY-----VVNQG 230
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
349-553 1.36e-09

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 59.03  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIRehFAVAFQE----------- 415
Cdd:PRK15112   29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFGDYSYRSQR--IRMIFQDpstslnprqri 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENiTDEEIYKSLENVYLL-DFVNQVgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK15112  107 SQILDFPLRLNTDLEPEQ-REKQIIETLRQVGLLpDHASYY---------PHMLAPGQKQRLGLARALILRPKVIIADEA 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 495 TAGLDIKTTN---NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK15112  177 LASLDMSMRSqliNLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
362-536 1.38e-09

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: 58.00  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 362 TLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVAFqehhifnlsiRDNFKMLYENITDEEIY 440
Cdd:cd03240    25 TLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIrEGEVRAQVKLAF----------ENANGKKYTITRSLAIL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 441 kslENVYlldFVNQVGLDYIVGNDGNKLSGGQK------HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKY 514
Cdd:cd03240    95 ---ENVI---FCHQGESNWPLLDMRGRCSGGEKvlasliIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEER 168
                         170       180
                  ....*....|....*....|....*
gi 2674892663 515 QKQT---MIVTSHDISLLRFFDDII 536
Cdd:cd03240   169 KSQKnfqLIVITHDEELVDAADHIY 193
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
349-552 1.45e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 60.64  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI-----FIQGKNYD--DLAEKSIRE-------HFAVAFQ 414
Cdd:PRK10261   32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQviELSEQSAAQmrhvrgaDMAMIFQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 E-----HHIFNL------SIRdnfkmLYENITDEEiyKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK10261  112 EpmtslNPVFTVgeqiaeSIR-----LHQGASREE--AMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQT---MIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK10261  185 CRPAVLIADEPTTALDVTIQAQIL-QLIKVLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
355-537 1.67e-09

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 60.57  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 355 SIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaEKSIRehfaVAFQEHHI---FNLSIRDNFKMLY 431
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK----ISYKPQYIspdYDGTVEEFLRSAN 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 432 ENITDEEIYKSlenvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD----IKTTNNIc 507
Cdd:COG1245   427 TDDFGSSYYKT-------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAI- 498
                         170       180       190
                  ....*....|....*....|....*....|
gi 2674892663 508 SQLMEKYQKQTMIVtSHDISLLRFFDDIII 537
Cdd:COG1245   499 RRFAENRGKTAMVV-DHDIYLIDYISDRLM 527
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
341-502 2.13e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 60.13  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaekSIREHFAVAFQEHHIFN 420
Cdd:PRK11819  333 SFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGETVKLAYVDQSRDA 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LsirDNFKMLYENITDeeiykslenvylldfvnqvGLDYI-VGN-----------------DGNK----LSGGQKHRLQL 478
Cdd:PRK11819  399 L---DPNKTVWEEISG-------------------GLDIIkVGNreipsrayvgrfnfkggDQQKkvgvLSGGERNRLHL 456
                         170       180
                  ....*....|....*....|....
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKT 502
Cdd:PRK11819  457 AKTLKQGGNVLLLDEPTNDLDVET 480
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
349-547 2.44e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 58.82  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN---YDDLAEKSIREHFAVAFQehhifNLSIR 424
Cdd:PRK11308   31 LDGVSFTLERG-KTLaVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkADPEAQKLLRQKIQIVFQ-----NPYGS 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DNFKMLYENITDE--EIYKSL------ENVylLDFVNQVGLD------YivgndGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK11308  105 LNPRKKVGQILEEplLINTSLsaaerrEKA--LAMMAKVGLRpehydrY-----PHMFSGGQRQRIAIARALMLDPDVVV 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 491 LDEPTAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:PRK11308  178 ADEPVSALDV----SVQAQvlnLMMDLQQElglSYVFISHDLSVVEHIaDEVMVMYLGRCVEKG 237
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
335-530 2.63e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 59.80  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknydDLAeKSIREHFavaF 413
Cdd:PRK10636  313 LKMEKVSAGYgDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLA-KGIKLGY---F 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENvYLLDFvnqvgldyivGNDGNKL-------SGGQKHRLQLAICLAKQK 486
Cdd:PRK10636  381 AQHQLEFLRADESPLQHLARLAPQELEQKLRD-YLGGF----------GFQGDKVteetrrfSGGEKARLVLALIVWQRP 449
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHDISLLR 530
Cdd:PRK10636  450 NLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLR 491
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
345-543 3.09e-09

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: 56.39  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRlLYPL-KGNIfiqgknyddlaekSIREHFAVAF--QEHHIFNL 421
Cdd:cd03223    13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRI-------------GMPEGEDLLFlpQRPYLPLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNFkmlyenitdeeiykslenVYLLDFVnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03223    79 TLREQL------------------IYPWDDV---------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2674892663 502 TTNNICSQLMEKyqKQTMIVTSHDISLLRFFDDII-ICGEEKI 543
Cdd:cd03223   126 SEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLdLDGEGGW 166
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
347-531 5.31e-09

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: 58.99  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLYPLKGNIF-IQGKNYDDLAeksirehfavAFQEHH 417
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFyVPQRPYMTLG----------TLRDQI 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKmlyENITDEEIYKSLENVYLLDFVNQ-VGLDyIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:TIGR00954 536 IYPDSSEDMKR---RGLSDKDLEQILDNVQLTHILEReGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2674892663 497 GLDIKTTNNICSQLMEKyqKQTMIVTSHDISLLRF 531
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKY 644
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
334-558 5.36e-09

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 57.02  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP----LKGNIFIQGKnydDLAEKSIR-EH 408
Cdd:PRK10418    4 QIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRgRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAV-------AFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDfvnqvgLDYIVGNDGNKLSGGQKHRLQLAIC 481
Cdd:PRK10418   81 IATimqnprsAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLEN------AARVLKLYPFEMSGGMLQRMMIALA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQT--MIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLREDS 558
Cdd:PRK10418  155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKH 234
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
342-556 8.07e-09

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 57.12  E-value: 8.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSiREHFAVAFQEHHIF-N 420
Cdd:PRK13537   17 YG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLDpD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKML--YENITDEEIYKSLENvyLLDFVN-QVGLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:PRK13537   95 FTVRENLLVFgrYFGLSAAAARALVPP--LLEFAKlENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 498 LDIKTTNNICSQLMEKYQK-QTMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLRE 556
Cdd:PRK13537  169 LDPQARHLMWERLRSLLARgKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
342-552 8.11e-09

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 57.04  E-value: 8.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlaeksirehfavafqehhifnl 421
Cdd:COG4152    11 FG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---------------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNF-----------KM------LY----ENITDEEIYKSLEnvYLLDfvnQVGL-DYIvgNDG-NKLSGGQKHRLQL 478
Cdd:COG4152    68 EDRRRIgylpeerglypKMkvgeqlVYlarlKGLSKAEAKRRAD--EWLE---RLGLgDRA--NKKvEELSKGNQQKVQL 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:COG4152   141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
PLN03073 PLN03073
ABC transporter F family; Provisional
339-529 1.13e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 57.95  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFiqgknyddlaeKSIREHFAVaFQEH 416
Cdd:PLN03073  513 DASFGYpgGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAV-FSQH 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNfKMLYenitdeeIYKSLENVYLLDFVNQVGLDYIVGNDGNK----LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PLN03073  581 HVDGLDLSSN-PLLY-------MMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLD 652
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2674892663 493 EPTAGLDIKTTNNICSQLMeKYQKQTMIVtSHDISLL 529
Cdd:PLN03073  653 EPSNHLDLDAVEALIQGLV-LFQGGVLMV-SHDEHLI 687
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
341-534 1.31e-08

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: 57.64  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLA-------EKSIREHFAVA 412
Cdd:TIGR03719  13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPqepqldpTKTVRENVEEG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEhhifNLSIRDNFKMLYENITDE------------EIYKSLENVYLLDFVNQVGL----------DYIVgndgNKLSG 470
Cdd:TIGR03719  93 VAE----IKDALDRFNEISAKYAEPdadfdklaaeqaELQEIIDAADAWDLDSQLEIamdalrcppwDADV----TKLSG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDD 534
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-----AWLERHLQEypgTVVAVTHD----RYFLD 222
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
448-536 1.93e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.13  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 448 LLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS 527
Cdd:PRK13409  193 LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLA 272

                  ....*....
gi 2674892663 528 LLRFFDDII 536
Cdd:PRK13409  273 VLDYLADNV 281
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
348-551 2.22e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.43  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKgnIFIQGK-NYDDLAEKSIREHFA-----VAFQEHHIFNL 421
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFH--IGVEGViTYDGITPEEIKKHYRgdvvyNAETDVHFPHL 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  422 SIRDNFKML---------YENITDEEIYKSLENVYLLDFvnqvGLDY----IVGNDGNK-LSGGQKHRLQLAICLAKQKD 487
Cdd:TIGR00956  154 TVGETLDFAarcktpqnrPDGVSREEYAKHIADVYMATY----GLSHtrntKVGNDFVRgVSGGERKRVSIAEASLGGAK 229
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  488 IILLDEPTAGLDIKTTNNI--CSQLMEKYQKQTMIVT----SHDISLLrfFDDIIICGEEKIIEQGNIKK 551
Cdd:TIGR00956  230 IQCWDNATRGLDSATALEFirALKTSANILDTTPLVAiyqcSQDAYEL--FDKVIVLYEGYQIYFGPADK 297
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
326-512 2.31e-08

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 56.57  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 326 EDKQSKDVQLLLKDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK 403
Cdd:COG3845   249 APAEPGEVVLEVENLSVRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHfAVAF--QEHH----IFNLSIRDNfkMLYENITDEEIYKSLenvyLLDF---------------VNQVGLDYIVG 462
Cdd:COG3845   329 ERRRL-GVAYipEDRLgrglVPDMSVAEN--LILGRYRRPPFSRGG----FLDRkairafaeelieefdVRTPGPDTPAR 401
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 463 NdgnkLSGG--QKhrLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME 512
Cdd:COG3845   402 S----LSGGnqQK--VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
352-525 2.31e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 55.32  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLfyvLMRL--LYPLKGNIFIQGKNYDDLAEKSIREHFA-VAFQEHHIFNLSIrdnFK 428
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPV---FQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 ML----YENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLA-ICLAKQKDI------ILLDEPTAG 497
Cdd:PRK03695   89 YLtlhqPDKTRTEAVASALNEV-----AEALGLDDKLGRSVNQLSGGEWQRVRLAaVVLQVWPDInpagqlLLLDEPMNS 163
                         170       180       190
                  ....*....|....*....|....*....|
gi 2674892663 498 LDIkTTNNICSQLMEKYQKQ--TMIVTSHD 525
Cdd:PRK03695  164 LDV-AQQAALDRLLSELCQQgiAVVMSSHD 192
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
349-536 2.73e-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: 54.57  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYvlmrllyplkGNIFIQG-KNYDDLAEKSIReHFAVAFQE---HHIFNLS-- 422
Cdd:cd03270    11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF----------DTIYAEGqRRYVESLSAYAR-QFLGQMDKpdvDSIEGLSpa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 -------IRDNFKMLYENITdeEIYKSLENVYL-------LDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03270    80 iaidqktTSRNPRSTVGTVT--EIYDYLRLLFArvgirerLGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IIL--LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:cd03270   158 GVLyvLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVI 209
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
357-536 2.77e-08

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: 56.72  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNifiqgknYDDLAEKS-IREHFA-VAFQEHhifnlsirdnFKMLYENi 434
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-------YDEEPSWDeVLKRFRgTELQDY----------FKKLANG- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 435 tdeEI---YKS-----------------LENV----YLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:COG1245   159 ---EIkvaHKPqyvdlipkvfkgtvrelLEKVdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLME--KYQKQTMIVtSHDISLLRFFDDII 536
Cdd:COG1245   236 FDEPSSYLDIYQRLNVARLIRElaEEGKYVLVV-EHDLAILDYLADYV 282
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
351-499 3.14e-08

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: 55.88  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF-NLSIR 424
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYVFQEARLFpHLSVR 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 425 DNFKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:COG4148    96 GNLLYGRKRAPRAERRISFDEV-----VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
346-547 3.52e-08

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 56.21  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLYPLK--GNIFIQGKNYDdlaEKSIREHFAVAfQEHHIF--N 420
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKgsGSVLLNGMPID---AKEMRAISAYV-QQDDLFipT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN------FKMlyenitDEEIYKSLENVYLLDFVNQVGL----DYIVGNDGNK--LSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR00955 114 LTVREHlmfqahLRM------PRRVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSseLFELFDKIILMAEGRVAYLG 249
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
335-525 4.07e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.05  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI----------FIQGKNYDDLAEK 403
Cdd:PRK15064  320 LEVENLTKGFDnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyYAQDHAYDFENDL 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQEHHIfNLSIRDNF-KMLYeniTDEEIYKSLENvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICL 482
Cdd:PRK15064  400 TLFDWMSQWRQEGDD-EQAVRGTLgRLLF---SQDDIKKSVKV----------------------LSGGEKGRMLFGKLM 453
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2674892663 483 AKQKDIILLDEPTAGLD---IKTTNNIcsqlMEKYqKQTMIVTSHD 525
Cdd:PRK15064  454 MQKPNVLVMDEPTNHMDmesIESLNMA----LEKY-EGTLIFVSHD 494
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
467-537 6.34e-08

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: 52.57  E-value: 6.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 467 KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC---SQLMEKYQKqTMIVTSHDISLLRFFDDIII 537
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAraiRRLSEEGKK-TALVVEHDLAVLDYLSDRIH 143
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
349-547 6.94e-08

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: 52.71  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlmrllyplkgnifiqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------VNEGLYASGKARLISFLPKFSRNK 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYenitdeeiykslenVYLLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKD--IILLDEPTAGLDikttNN 505
Cdd:cd03238    62 LIF--------------IDQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH----QQ 123
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 506 ICSQLMEKY-----QKQTMIVTSHDISLLRFFDDIIICGE------EKIIEQG 547
Cdd:cd03238   124 DINQLLEVIkglidLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
350-534 7.80e-08

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 54.33  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 350 KDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQEhHIFNLS---- 422
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQD-PLASLNprmt 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 ----IRDNFKMLYENITDEEIYKSLENVYLldfvnQVGLdyiVGNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK15079  117 igeiIAEPLRTYHPKLSRQEVKDRVKAMML-----KVGL---LPNLINRypheFSGGQCQRIGIARALILEPKLIICDEP 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2674892663 495 TAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFFDD 534
Cdd:PRK15079  189 VSALDV----SIQAQvvnLLQQLQREmglSLIFIAHDLAVVKHISD 230
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
335-530 1.05e-07

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 53.27  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDL--AYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD------------DL 400
Cdd:COG4598     9 LEVRDLhkSFGDLEVL-KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpaDR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 401 AE-KSIREHFAVAFQEhhiFNL----SIRdnfkmlyENIT-----------DEEIYKSLEnvyLLDfvnQVGL----DYI 460
Cdd:COG4598    88 RQlQRIRTRLGMVFQS---FNLwshmTVL-------ENVIeapvhvlgrpkAEAIERAEA---LLA---KVGLadkrDAY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 461 VGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD----------IKttnnicsQLMEkyQKQTMIVTSHDISLLR 530
Cdd:COG4598   152 PAH----LSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelvgevlkvMR-------DLAE--EGRTMLVVTHEMGFAR 218
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
349-498 1.61e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 54.16  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYP---LKGNIFIQGKnydDLAEKSIREH----FAVAFQEHHIF-N 420
Cdd:PRK13549   21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPhgtYEGEIIFEGE---ELQASNIRDTeragIAIIHQELALVkE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYE-----NITDEEIYksLENVYLLdfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13549   97 LSVLENIFLGNEitpggIMDYDAMY--LRAQKLL---AQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171

                  ...
gi 2674892663 496 AGL 498
Cdd:PRK13549  172 ASL 174
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
349-499 4.09e-07

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 52.71  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLL---YPL-KGNIFIQGKNYDDLAEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:COG1129    20 LDGVSLELRPGEVHALLGENGAGKSTL----MKILsgvYQPdSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYEN-----ITDEEIYKSLENvyLLDfvnQVGLDY----IVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG1129    96 VAENIFLGREPrrgglIDWRAMRRRARE--LLA---RLGLDIdpdtPVGD----LSVAQQQLVEIARALSRDARVLILDE 166

                  ....*.
gi 2674892663 494 PTAGLD 499
Cdd:COG1129   167 PTASLT 172
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
340-530 4.26e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 52.65  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLY------------PLKGnifIQGKNYDD 399
Cdd:PRK11147   11 LSFS-DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgRIIYeqdlivarlqqdPPRN---VEGTVYDF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE--KSIREHFAvafQEHHIFNLSIRD-NFKMLYENitdEEIYKSLE--NVYLLDF-VNQV----GLDyivgNDG--NK 467
Cdd:PRK11147   87 VAEgiEEQAEYLK---RYHDISHLVETDpSEKNLNEL---AKLQEQLDhhNLWQLENrINEVlaqlGLD----PDAalSS 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 468 LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDISLLR 530
Cdd:PRK11147  157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-----EWLEGFLKTfqgSIIFISHDRSFIR 217
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
349-525 5.74e-07

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: 50.90  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLLY----PLKGNIFIQ-GKNYDDLAEKSirehfavafqEHHIfnLSI 423
Cdd:COG4778    27 LDGVSFSVAAGECVALTGPSGAGKSTL----LKCIYgnylPDSGSILVRhDGGWVDLAQAS----------PREI--LAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNfkmlyenitdeEI-YKS-----LENVYLLDFVNQVGLDYIVGNDG-----------------------NKLSGGQKH 474
Cdd:COG4778    91 RRR-----------TIgYVSqflrvIPRVSALDVVAEPLLERGVDREEarararellarlnlperlwdlppATFSGGEQQ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHD 525
Cdd:COG4778   160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVV-ELIEEAKARgtAIIGIFHD 211
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
334-501 7.31e-07

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 51.38  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYD-KVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPLK----GNIFIQGKNYDDL--AEKSI 405
Cdd:PRK11650    3 GLKLQAVRKSYDgKTQvIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGLEritsGEIWIGGRVVNELepADRDI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 406 rehfAVAFQEH----HifnLSIRDNfkMLY---------ENITD--EEIYKSLENVYLLDfvnqvgldyivgNDGNKLSG 470
Cdd:PRK11650   79 ----AMVFQNYalypH---MSVREN--MAYglkirgmpkAEIEErvAEAARILELEPLLD------------RKPRELSG 137
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:PRK11650  138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
346-536 8.74e-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: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFyvlmrllyplkgnifiqgknyDDLAeksirehFAVAFQEHHIFnlsird 425
Cdd:cd03227     8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTIL---------------------DAIG-------LALGGAQSATR------ 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 nfKMLYENITDEEIYKSLENVYLLDfvnqvgldyivgndgnKLSGGQKHRLQLAICLAKQK----DIILLDEPTAGLDIK 501
Cdd:cd03227    54 --RRSGVKAGCIVAAVSAELIFTRL----------------QLSGGEKELSALALILALASlkprPLYILDEIDRGLDPR 115
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2674892663 502 TTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDII 536
Cdd:cd03227   116 DGQALAEAILEHLVKGaQVIVITHLPELAELADKLI 151
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
341-534 1.02e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 51.66  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQgKNY-----------DDlaEKSIREHF 409
Cdd:PRK11819   15 VVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIkvgylpqepqlDP--EKTVRENV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEhhIFNLsiRDNFKMLYENITDEEIYKS--------LENvyLLDFVNQVGLDYIV------------GNDGNKLS 469
Cdd:PRK11819   92 EEGVAE--VKAA--LDRFNEIYAAYAEPDADFDalaaeqgeLQE--IIDAADAWDLDSQLeiamdalrcppwDAKVTKLS 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 470 GGQKHRLqlAIC--LAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDD 534
Cdd:PRK11819  166 GGERRRV--ALCrlLLEKPDMLLLDEPTNHLDAESV-----AWLEQFLHDypgTVVAVTHD----RYFLD 224
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
335-499 1.46e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 49.10  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIrehfavAFQ 414
Cdd:PRK13541    2 LSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC------TYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHI---FNLSIRDNFKMLyenitdEEIYKSLENVYLLdfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK13541   76 GHNLglkLEMTVFENLKFW------SEIYNSAETLYAA--IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147

                  ....*...
gi 2674892663 492 DEPTAGLD 499
Cdd:PRK13541  148 DEVETNLS 155
PLN03140 PLN03140
ABC transporter G family member; Provisional
348-499 1.46e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 51.39  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQG--KNYDDLA------EKSIREHFAVAFQEHH 417
Cdd:PLN03140   895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpKKQETFArisgycEQNDIHSPQVTVRESL 974
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  418 IFNLSIRdnfkmLYENITDEEIYKSLENVylLDFVNQVGL-DYIVGNDG-NKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PLN03140   975 IYSAFLR-----LPKEVSKEEKMMFVDEV--MELVELDNLkDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047

                   ....
gi 2674892663  496 AGLD 499
Cdd:PLN03140  1048 SGLD 1051
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
333-498 1.46e-06

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 49.49  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 333 VQLLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI-REHFA 410
Cdd:PRK11614    4 VMLSFDKVSAHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImREAVA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFN-LSIRDNFKMLYENITDEEIYKSLENVYLLdFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11614   84 IVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWVYEL-FPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159

                  ....*....
gi 2674892663 490 LLDEPTAGL 498
Cdd:PRK11614  160 LLDEPSLGL 168
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
352-547 1.50e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 50.51  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-YPLK---GNIFIQGKNYDDLAEKSIRE----HFAVAFQEHHI-FNLS 422
Cdd:PRK11022   26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRvmaEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTsLNPC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDFVNQVG-------LDyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK11022  106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrLD----VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLL-RFFDDIIICGEEKIIEQG 547
Cdd:PRK11022  182 TALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETG 236
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
349-500 1.53e-06

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 50.79  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNktlIVGTSG---CGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREhfA----VAF-----QEH 416
Cdd:COG1129   268 VRDVSFSVRAGE---ILGIAGlvgAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRD--AiragIAYvpedrKGE 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF-NLSIRDNFkmlyeNITdeeIYKSLENVYLLDF--VNQVGLDYI-------------VGNdgnkLSGG--QKhrLQL 478
Cdd:COG1129   340 GLVlDLSIRENI-----TLA---SLDRLSRGGLLDRrrERALAEEYIkrlriktpspeqpVGN----LSGGnqQK--VVL 405
                         170       180
                  ....*....|....*....|..
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDI 500
Cdd:COG1129   406 AKWLATDPKVLILDEPTRGIDV 427
hmuV PRK13547
heme ABC transporter ATP-binding protein;
346-553 2.06e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 49.44  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL--------YPLKGNIFIQGKNYDDL-AEKSIREHFAVAFQEH 416
Cdd:PRK13547   14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIdAPRLARLRAVLPQAAQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNFKM-LYEN--------ITDEEI-YKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAK-- 484
Cdd:PRK13547   94 PAFAFSAREIVLLgRYPHarragaltHRDGEIaWQALA---------LAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 485 -----QKD--IILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISL-LRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13547  165 pphdaAQPprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
353-525 2.22e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 50.28  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 353 NLSIK--KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-----GKNYDDlaeksireHFAvaFQEHHIFNLSI-- 423
Cdd:PRK15064   19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQD--------QFA--FEEFTVLDTVImg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 ----------RDNFKMLYEnITDEEIYK--SLENVY---------------LLdfvnQVGLDyIVGNDG--NKLSGGQKH 474
Cdd:PRK15064   89 htelwevkqeRDRIYALPE-MSEEDGMKvaDLEVKFaemdgytaearagelLL----GVGIP-EEQHYGlmSEVAPGWKL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHD 525
Cdd:PRK15064  163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIIISHD 211
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
349-529 3.71e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 49.85  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE---KSIREHFAVAFQE-------HHI 418
Cdd:PRK10261  340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyasldpRQT 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFK---MLYENITDEEIYKSLENVYLLDfvnQVGLDYivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK10261  420 VGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLLP---EHAWRY-----PHEFSGGQRQRICIARALALNPKVIIADEAV 491
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2674892663 496 AGLDIKTTNNICSQLMEkYQKQ---TMIVTSHDISLL 529
Cdd:PRK10261  492 SALDVSIRGQIINLLLD-LQRDfgiAYLFISHDMAVV 527
PLN03140 PLN03140
ABC transporter G family member; Provisional
348-547 6.18e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.46  E-value: 6.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-----------RLLY---------PLKGNIFIQ-------------- 393
Cdd:PLN03140   180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgkldpslkvsgEITYngyrlnefvPRKTSAYISqndvhvgvmtvket 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  394 ----------GKNYDDLAEKSIREHFAVAFQEHHIfnlsirdnfKMLYENITDEEIYKSLENVYLLDFVnqvGLDY---- 459
Cdd:PLN03140   260 ldfsarcqgvGTRYDLLSELARREKDAGIFPEAEV---------DLFMKATAMEGVKSSLITDYTLKIL---GLDIckdt 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  460 IVGNDGNK-LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI--CSQLMEKYQKQTMIVtshdiSLLR------ 530
Cdd:PLN03140   328 IVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkCLQQIVHLTEATVLM-----SLLQpapetf 402
                          250
                   ....*....|....*...
gi 2674892663  531 -FFDDIIICGEEKIIEQG 547
Cdd:PLN03140   403 dLFDDIILLSEGQIVYQG 420
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
347-530 7.08e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 48.89  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaeKSIREH----FAVAfQEHHIF-NL 421
Cdd:PRK15439   25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL--TPAKAHqlgiYLVP-QEPLLFpNL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNfkMLYENITDEEIYKSLENvyLLDFVN-QVGLDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:PRK15439  102 SVKEN--ILFGLPKRQASMQKMKQ--LLAALGcQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2674892663 501 KTTNNICSQLMEKYQKQTMIV-TSHDISLLR 530
Cdd:PRK15439  174 AETERLFSRIRELLAQGVGIVfISHKLPEIR 204
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
389-561 9.51e-06

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: 48.86  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 389 NIFIQGKNYDDLAEKSIREhfavafqEHHIFNLSIRDNFKmlyENITDE---EIYKSLEnvYLLDfvnqVGLDYI-VGND 464
Cdd:TIGR00630 422 AVTVGGKSIADVSELSIRE-------AHEFFNQLTLTPEE---KKIAEEvlkEIRERLG--FLID----VGLDYLsLSRA 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 465 GNKLSGGQKHRLQLAICLAKQKDIIL--LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII----- 536
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRlRDLGNTLIVVEHDEDTIRAADYVIdigpg 565
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2674892663 537 --ICGEEkIIEQGNIKKLLLREDS----YLN 561
Cdd:TIGR00630 566 agEHGGE-VVASGTPEEILANPDSltgqYLS 595
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
346-549 1.08e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 48.24  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlmrlLYPLKGNIFIQGKNYddlaekSIREHFAVAF--QEHHIFNLSI 423
Cdd:PRK10636   14 RVLLDNATATINPGQKVGLVGKNGCGKSTL-------LALLKNEISADGGSY------TFPGNWQLAWvnQETPALPQPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDnfkmlYENITDEEiYKSLENVylLDFVNQVgldyivgNDGN-------KL---------------------------- 468
Cdd:PRK10636   81 LE-----YVIDGDRE-YRQLEAQ--LHDANER-------NDGHaiatihgKLdaidawtirsraasllhglgfsneqler 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 -----SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDDIIIcge 540
Cdd:PRK10636  146 pvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV-----IWLEKWLKSyqgTLILISHD----RDFLDPIV--- 213
                         250
                  ....*....|.
gi 2674892663 541 EKI--IEQGNI 549
Cdd:PRK10636  214 DKIihIEQQSL 224
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
358-537 1.47e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.06  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  358 KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIqgknyddlaeksirehfavafqehhifnlsirdnfkmlyenITDE 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  438 EIYKSLENVYLLDfvnqvgldyIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL------- 510
Cdd:smart00382  40 DILEEVLDQLLLI---------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllll 110
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2674892663  511 MEKYQKQTMIVTSHDIS------LLRFFDDIII 537
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpalLRRRFDRRIV 143
PLN03211 PLN03211
ABC transporter G-25; Provisional
345-547 2.93e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.80  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP--LKGNIFIQGKNyddLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PLN03211   80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRK---PTKQILKRTGFVTQDDILYPHLT 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKM-----LYENITDEEIYKSLENVylldfVNQVGL----DYIVGNDGNK-LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PLN03211  157 VRETLVFcsllrLPKSLTKQEKILVAESV-----ISELGLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 493 EPTAGLDIKTTNNICSQLMEKYQKQTMIVTS-HDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:PLN03211  232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSsrVYQMFDSVLVLSEGRCLFFG 289
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
455-541 4.13e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.75  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  455 VGLDYI-VGNDGNKLSGGQKHRLQLAICL---AKQKDIILLDEPTAGL---DIKTTNNICSQLMekYQKQTMIVTSHDIS 527
Cdd:PRK00635   796 LGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYVLQSLT--HQGHTVVIIEHNMH 873
                           90
                   ....*....|....
gi 2674892663  528 LLRFFDDIIICGEE 541
Cdd:PRK00635   874 VVKVADYVLELGPE 887
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
449-541 4.86e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.36  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  449 LDFVNQVGLDYIV-GNDGNKLSGGQKHRLQLAICLAKQ-KDII-LLDEPTAGLDIKTTNNICSQLMEKY-QKQTMIVTSH 524
Cdd:PRK00635  1368 LTFIDKVGLSYITlGQEQDTLSDGEHYRLHLAKKISSNlTDIIyLLEDPLSGLHPQDAPTLLQLIKELVtNNNTVIATDR 1447
                           90
                   ....*....|....*..
gi 2674892663  525 DISLLRFFDDIIICGEE 541
Cdd:PRK00635  1448 SGSLAEHADHLIHLGPG 1464
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
16-259 6.22e-05

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 45.23  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  16 LLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVLI 95
Cdd:cd07346     1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  96 KIIKaLP--FKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPYM 173
Cdd:cd07346    81 HLQR-LSlsFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 174 ---IWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVI 250
Cdd:cd07346   160 rrrIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239

                  ....*....
gi 2674892663 251 CLAISIYLV 259
Cdd:cd07346   240 VLLYGGYLV 248
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
349-503 7.29e-05

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: 45.59  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYP---LKGNIFIQGKnydDLAEKSIREH----FAVAFQEHHIF-N 420
Cdd:TIGR02633  17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPhgtWDGEIYWSGS---PLKASNIRDTeragIVIIHQELTLVpE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYEnIT-------DEEIYKSLENVylldfVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:TIGR02633  93 LSVAENIFLGNE-ITlpggrmaYNAMYLRAKNL-----LRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
                         170
                  ....*....|.
gi 2674892663 493 EPTAGLDIKTT 503
Cdd:TIGR02633 167 EPSSSLTEKET 177
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
349-498 1.11e-04

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 45.02  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLY----PLKGNIFIQGKnyddlaEKSIRE-HFAVA------FQeHh 417
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKST----LMKILYglyqPDSGEILIDGK------PVRIRSpRDAIAlgigmvHQ-H- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 iFnlsirdnfkMLYENITdeeiykSLENVYL-------------------LDFVNQVGL----DYIVGNdgnkLSGGQKH 474
Cdd:COG3845    89 -F---------MLVPNLT------VAENIVLgleptkggrldrkaarariRELSERYGLdvdpDAKVED----LSVGEQQ 148
                         170       180
                  ....*....|....*....|....
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGL 498
Cdd:COG3845   149 RVEILKALYRGARILILDEPTAVL 172
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
394-501 1.28e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 45.02  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 394 GKNYDDLAEKSIREhfAVAFqehhifnlsirdnFkmlyENITdeEIYKSLEnvYLLDfvnqVGLDYI-VGNDGNKLSGGQ 472
Cdd:COG0178   779 GKNIADVLDMTVEE--ALEF-------------F----ENIP--KIARKLQ--TLQD----VGLGYIkLGQPATTLSGGE 831
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2674892663 473 KHRLQLAICLAK---QKDIILLDEPTAGL---DIK 501
Cdd:COG0178   832 AQRVKLASELSKrstGKTLYILDEPTTGLhfhDIR 866
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
450-552 1.93e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 43.96  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 450 DFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDIS 527
Cdd:NF000106  127 ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrsMVRDGATVLLTTQYMEE 206
                          90       100
                  ....*....|....*....|....*
gi 2674892663 528 LLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:NF000106  207 AEQLAHELTVIDRGRVIADGKVDEL 231
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
349-551 3.21e-04

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 42.88  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyddlaeksirEHFAVAFQEHHIFNLSIRDN-- 426
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENie 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMLYENITDEEIYKSLENVY----LLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKIIefseLGEFIYQ---------PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNICSQLME-KYQKQTMIVTSHDISLLRFFddiiiCGEEKIIEQGNIKK 551
Cdd:PRK13546  179 AQKCLDKIYEfKEQNKTIFFVSHNLGQVRQF-----CTKIAWIEGGKLKD 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
351-547 4.93e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 42.22  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:PRK11701   24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLYALSEAERRRLLRTEWGFVHQHPRDGLR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 ML------------------YENITDEEiykslenvylLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11701  104 MQvsaggnigerlmavgarhYGDIRATA----------GDWLERVEIDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 490 LLDEPTAGLDIKTTN---NICSQLMEKYQKQTMIVTsHDISLLRFFDD-IIICGEEKIIEQG 547
Cdd:PRK11701  174 FMDEPTGGLDVSVQArllDLLRGLVRELGLAVVIVT-HDLAVARLLAHrLLVMKQGRVVESG 234
uvrA PRK00349
excinuclease ABC subunit UvrA;
449-501 6.60e-04

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 6.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 449 LDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPTAGL---DIK 501
Cdd:PRK00349  811 LQTLVDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLhfeDIR 870
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
468-565 7.27e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 42.35  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 468 LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIIcgeekIIE 545
Cdd:PRK15439  404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI-YQLIRSIAAQnvAVLFISSDLEEIEQMADRVL-----VMH 477
                          90       100
                  ....*....|....*....|
gi 2674892663 546 QGNIKKLLLREDSYLNKLIR 565
Cdd:PRK15439  478 QGEISGALTGAAINVDTIMR 497
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
349-552 1.02e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.02  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH-FAVAFQE-HHIFNLSIRDN 426
Cdd:PRK10982   14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQElNLVLQRSVMDN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F-------KMLYenITDEEIYKSLENVYlldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK10982   94 MwlgryptKGMF--VDQDKMYRDTKAIF-----DELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 IKTTNNICSqLMEKYQKQ--TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK10982  167 EKEVNHLFT-IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWIATQPLAGL 221
AAA_29 pfam13555
P-loop containing region of AAA domain;
358-391 1.04e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 37.58  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2674892663 358 KGNkTLIVGTSGCGKSTLFYVLMRLLYPLKGNIF 391
Cdd:pfam13555  22 RGN-TLLTGPSGSGKSTLLDAIQTLLVPAKRARF 54
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
21-175 1.40e-03

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 40.88  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  21 LVGTISTLSSISLMGLSAWLIASA-------ALQPPLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVFV 93
Cdd:cd18542     2 LLAILALLLATALNLLIPLLIRRIidsviggGLRELLWLLALLILGV---ALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  94 LIKIIKaLPF----KQQTenGDAFDLIVNAVDNLRDsFLRFFLPPIITTISVFILSIWfflysydlmILLISSW---LIF 166
Cdd:cd18542    79 YDHLQR-LSFsfhdKART--GDLMSRCTSDVDTIRR-FLAFGLVELVRAVLLFIGALI---------IMFSINWkltLIS 145

                  ....*....
gi 2674892663 167 MIVIPYMIW 175
Cdd:cd18542   146 LAIIPFIAL 154
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
351-543 1.44e-03

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: 41.35  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLK--GNIFIQGKNYD-DLAEKSIREHFAVAFQEH----------- 416
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGKfeGNVFINGKPVDiRNPAQAIRAGIAMVPEDRkrhgivpilgv 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 -HIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDfVNQVGLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR02633 357 gKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLK-VKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKI 543
Cdd:TIGR02633 432 RGVDVGAKYEI-YKLINQLAQEgvAIIVVSSELAeVLGLSDRVLVIGEGKL 481
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
15-280 1.80e-03

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 40.32  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  15 SLLLAILVGTISTLSSISLMGLSAWLIASAALQP-PLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVFV 93
Cdd:pfam00664   4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETqALNVYSLALLLL---GLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  94 LIKIIKA-LPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPY 172
Cdd:pfam00664  81 FKKILRQpMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 173 ---MIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLV 249
Cdd:pfam00664 161 fakILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2674892663 250 ICLAISIYLVNTQDFNPIMAITIIlTYQAVL 280
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFL-SLFAQL 270
PLN03073 PLN03073
ABC transporter F family; Provisional
437-524 1.86e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.00  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 437 EEIYKSLEnvyLLDFVNQ--------VGLDY---IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:PLN03073  306 EEIYKRLE---LIDAYTAearaasilAGLSFtpeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLW 382
                          90
                  ....*....|....*....
gi 2674892663 506 ICSQLMeKYQKqTMIVTSH 524
Cdd:PLN03073  383 LETYLL-KWPK-TFIVVSH 399
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
16-175 1.93e-03

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 40.48  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  16 LLLAILVGTISTLSSISLMGLSAWLIASAALQPP---LYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVF 92
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDleaLLLVPLAIIGL---FLLRGLASYLQTYLMAYVGQRVVRDLRND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  93 VLIKIIKA-LPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMillisswLIFMIVIP 171
Cdd:cd18552    78 LFDKLLRLpLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLT-------LIALVVLP 150

                  ....
gi 2674892663 172 YMIW 175
Cdd:cd18552   151 LAAL 154
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
364-526 2.00e-03

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: 41.15  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaekSIREHFAVAFQehhifNLSIRDNFKMLYENITDEE---IY 440
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILTNISDVHQ-----NMGYCPQFDAIDDLLTGREhlyLY 2036
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663  441 KSLENVYLLDF-------VNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTT----NNICSQ 509
Cdd:TIGR01257 2037 ARLRGVPAEEIekvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSI 2116
                          170
                   ....*....|....*..
gi 2674892663  510 LMEkyqKQTMIVTSHDI 526
Cdd:TIGR01257 2117 IRE---GRAVVLTSHSM 2130
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
457-553 2.92e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 40.37  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 457 LDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQTM---IVTSHDISLLRFFD 533
Cdd:PRK10762  389 MEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI-YQLINQFKAEGLsiiLVSSEMPEVLGMSD 463
                          90       100
                  ....*....|....*....|....*
gi 2674892663 534 DIIICGEEKI-----IEQGNIKKLL 553
Cdd:PRK10762  464 RILVMHEGRIsgeftREQATQEKLM 488
uvrA PRK00349
excinuclease ABC subunit UvrA;
390-561 4.23e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 40.06  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 390 IFIQGKNYDDLAEKSIREhfAVAFQEhhifNLSIRDNFKMLYENITdEEIYKSLEnvylldFVNQVGLDYI-VGNDGNKL 468
Cdd:PRK00349  424 VKVGGKNIGEVSELSIGE--ALEFFE----NLKLSEQEAKIAEPIL-KEIRERLK------FLVDVGLDYLtLSRSAGTL 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRlqlaICLAKQkdI------IL--LDEPTAGL---D----IKTTNNicsqLMEKyqKQTMIVTSHDISLLRFFD 533
Cdd:PRK00349  491 SGGEAQR----IRLATQ--IgsgltgVLyvLDEPSIGLhqrDndrlIETLKH----LRDL--GNTLIVVEHDEDTIRAAD 558
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2674892663 534 DII-I---CGEE--KIIEQGNIKKLLLREDS----YLN 561
Cdd:PRK00349  559 YIVdIgpgAGVHggEVVASGTPEEIMKNPNSltgqYLS 596
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
349-537 8.84e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 38.94  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD-LAEKSIREHFAVAFQEHH---IF-NLSI 423
Cdd:PRK10982  264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAINHGFALVTEERRstgIYaYLDI 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 rdNFKMLYENITDeeiYKS----LENVYLLDFVNQVGLDYIVGNDGNK-----LSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK10982  344 --GFNSLISNIRN---YKNkvglLDNSRMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEP 418
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PRK10982  419 TRGIDVGAKFEIYQLIAElaKKDKGIIIISSEMPELLGITDRILV 463
 
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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