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Conserved domains on  [gi|1433048008|gb|AXF48661|]
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HisMBPTEV-GFP [Cloning vector pT7pelBMBPGFP]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
36-402 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 799.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  36 KTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 115
Cdd:PRK09474   27 KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 195
Cdd:PRK09474  107 PSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 196 IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 275
Cdd:PRK09474  187 IAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGI 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 276 NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT 355
Cdd:PRK09474  267 NYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAAT 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1433048008 356 MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:PRK09474  347 MDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
GFP super family cl08319
Green fluorescent protein;
431-614 7.26e-15

Green fluorescent protein;


The actual alignment was detected with superfamily member pfam01353:

Pssm-ID: 426217  Cd Length: 211  Bit Score: 73.76  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 431 LDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 509
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 510 TISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLeyNYNSHNVYITADKQKNGIKANFKIRHNIEDGS- 588
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSL--TGWDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180
                  ....*....|....*....|....*...
gi 1433048008 589 --VQLADHYQQNTPIGDGpVLLPDNHYL 614
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFV 186
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
36-402 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 799.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  36 KTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 115
Cdd:PRK09474   27 KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 195
Cdd:PRK09474  107 PSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 196 IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 275
Cdd:PRK09474  187 IAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGI 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 276 NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT 355
Cdd:PRK09474  267 NYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAAT 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1433048008 356 MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:PRK09474  347 MDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 40-402 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 703.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  40 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 119
Cdd:cd13656     1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 120 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 199
Cdd:cd13656    81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 200 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 279
Cdd:cd13656   161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 280 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 359
Cdd:cd13656   241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1433048008 360 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:cd13656   321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
36-402 9.96e-148

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 434.38  E-value: 9.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  36 KTEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAE 113
Cdd:COG2182    35 AGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 114 ITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFT 192
Cdd:COG2182   114 LDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYF 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 193 WPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT 272
Cdd:COG2182   194 YPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKK 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 273 S-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAK 348
Cdd:COG2182   272 AlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKA 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1433048008 349 DPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:COG2182   350 DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQ 403
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 57-350 3.42e-34

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 131.76  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  57 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 132
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 133 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 208
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 209 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 287
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1433048008 288 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 350
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
GFP pfam01353
Green fluorescent protein;
431-614 7.26e-15

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 73.76  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 431 LDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 509
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 510 TISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLeyNYNSHNVYITADKQKNGIKANFKIRHNIEDGS- 588
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSL--TGWDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180
                  ....*....|....*....|....*...
gi 1433048008 589 --VQLADHYQQNTPIGDGpVLLPDNHYL 614
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFV 186
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
36-402 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 799.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  36 KTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 115
Cdd:PRK09474   27 KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 195
Cdd:PRK09474  107 PSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 196 IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 275
Cdd:PRK09474  187 IAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGI 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 276 NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT 355
Cdd:PRK09474  267 NYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAAT 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1433048008 356 MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:PRK09474  347 MDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 40-402 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 703.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  40 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 119
Cdd:cd13656     1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 120 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 199
Cdd:cd13656    81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 200 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 279
Cdd:cd13656   161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 280 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 359
Cdd:cd13656   241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1433048008 360 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:cd13656   321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
36-402 9.96e-148

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 434.38  E-value: 9.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  36 KTEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAE 113
Cdd:COG2182    35 AGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 114 ITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFT 192
Cdd:COG2182   114 LDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYF 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 193 WPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT 272
Cdd:COG2182   194 YPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKK 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 273 S-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAK 348
Cdd:COG2182   272 AlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKA 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1433048008 349 DPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:COG2182   350 DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQ 403
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 41-402 7.40e-146

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 427.98  E-value: 7.40e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTVEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 116
Cdd:cd13522     1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 117 DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 195
Cdd:cd13522    81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 196 IAADGGYAFKYENGKYDIkdvGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID-TS 273
Cdd:cd13522   161 IGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRqAL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 274 KVNYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLeaVNKDKPLGAVALKSYEEELAKDPRI 352
Cdd:cd13522   238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1433048008 353 A--ATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:cd13522   316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 41-402 8.05e-135

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 399.75  E-value: 8.05e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 118
Cdd:cd13586     1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 119 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDK--ELKAKGKSALMFNLQEPYFTWPLI 196
Cdd:cd13586    81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQTNPYFSYPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 197 AADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 275
Cdd:cd13586   161 AAFGGYVFGENGG--DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 276 NYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPlGAVALKSYEE--ELAKDPRI 352
Cdd:cd13586   239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTG-RIPALKDALNdaAVKNDPLV 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1433048008 353 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:cd13586   317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAA 366
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 41-399 3.02e-87

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 277.06  E-value: 3.02e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 118
Cdd:cd13658     1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 119 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 196
Cdd:cd13658    81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 197 AADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVN 276
Cdd:cd13658   161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 277 YGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PlGAVALKSYEEElAKDPRI 352
Cdd:cd13658   241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiP-PRKDVRSDPEI-KNNPLT 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1433048008 353 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 399
Cdd:cd13658   318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDA 364
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 41-400 1.11e-72

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 238.82  E-value: 1.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT- 115
Cdd:cd13657     1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 ---PDKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPY 190
Cdd:cd13657    81 ylsEDDF--ENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 191 FTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 270
Cdd:cd13657   159 FVSAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 271 DTSKVNYGVTVLPTFKGQ-PSKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELA 347
Cdd:cd13657   233 KAAGIDLGVAPLPTVDGTnPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVA 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1433048008 348 KDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 400
Cdd:cd13657   313 ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 41-400 2.92e-58

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 201.09  E-value: 2.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKG-YNGLAEVGKKFEK-DTGIKVTVEhP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 115
Cdd:cd13585     1 TLTFWDWGQPAeTAALKKLIDAFEKeNPGVKVEVV-PvpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 P---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL------PNPPKTWEEIPALDKELKAKGKS----AL 182
Cdd:cd13585    80 DyieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLEAAKKLTDKKGGqygfAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 183 MFNLQEPYFTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGETAMT 260
Cdd:cd13585   160 RGGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMM 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 261 INGPWAWSNIDTSKV--NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG---LEAVNKDKPLG 335
Cdd:cd13585   235 IDGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALA 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1433048008 336 AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASG--RQTVDEALKDAQ 400
Cdd:cd13585   314 AAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAA 380
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 38-329 1.13e-55

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 193.34  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  38 EEGKLVIWINGDKGYNGLAEVGKKFEKDT-GIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 114
Cdd:COG1653    31 GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 115 TP----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAK-GKSALMFN 185
Cdd:COG1653   111 DDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEkaglDPPKTWDELLAAAKKLKAKdGVYGFALG 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 186 LQEPYFTWPLIAADGGYAFKyENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAMTIN 262
Cdd:COG1653   191 GKDGAAWLDLLLSAGGDLYD-EDGK-----PAFDSPEAVEALEFLKDLVKDGYVPPGalgTDWDDARAAFASGKAAMMIN 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 263 GPWAWSNIDTS--KVNYGVTVLPTFK-GQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 329
Cdd:COG1653   265 GSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKWD 333
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 41-401 1.36e-55

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 193.66  E-value: 1.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWI-NGDKGYNGLAEVGKKFEK-DTGIKVTVEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 115
Cdd:cd14748     1 EITFWHgMSGPDGKALEELVDEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 116 P----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-------PNPPKTWEEI----PALDKELKAKGKS 180
Cdd:cd14748    81 DyidkDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFeeagldpEKPPKTWDELeeaaKKLKDKGGKTGRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 181 ALMFNLQEPYFTW-PLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAM 259
Cdd:cd14748   161 GFALPPGDGGWTFqALLWQNGGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 260 TINGPWAWSNI--DTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDEGLEAVNKDK---P 333
Cdd:cd14748   236 TINGTWSLAGIrdKGAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylP 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1433048008 334 LGAVALKSYEEELAKDPRIAATMENAQKGE-IMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT 401
Cdd:cd14748   315 VRKSAAEDPEEFLAENPNYKVAVDQLDYAKpWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 50-400 9.88e-40

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 150.14  E-value: 9.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  50 KGYNGLAEVGKKFEKDT-GIKVTVE-HP---DKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITPD-- 117
Cdd:cd14750    11 QEGELLKKAIAAFEKKHpDIKVEIEeLPassDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEYlk 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 118 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAKGKSALMFNLQ----EP 189
Cdd:cd14750    87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 190 YFT--WPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGETAMTINGP 264
Cdd:cd14750   167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 265 WAW--SNIDTSKVN--YGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALK 340
Cdd:cd14750   242 YAYalLQGPESAVAgkVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1433048008 341 SYEEE--LAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 400
Cdd:cd14750   321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQ 382
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 41-402 1.82e-39

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 149.45  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 114
Cdd:cd14749     1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 115 TP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-----NPPKTWEEIPALDKELKAKGK------S 180
Cdd:cd14749    81 TDyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKgqtgfgL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 181 ALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKdvgvDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGET 257
Cdd:cd14749   161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFN----DPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 258 AMTINGPWAWSNIDTSKV--NYGVTVLPTFK--GQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEA-VNKDK 332
Cdd:cd14749   236 AMNIGGSWDLGAIKAGEPggKIGVFPFPTVGkgAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQyLEDVG 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1433048008 333 PLGAVALKSYEEELAKDPRIAATME-NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 402
Cdd:cd14749   315 LLPAKEVVAKDEDPDPVAILGPFADvLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSA 385
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 41-401 5.50e-39

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 148.23  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTVEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 112
Cdd:cd14747     1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 113 EITP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDKELKAKG--KSAL 182
Cdd:cd14747    77 DLTPyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLkkaggDEAPKTWDELEAAAKKIKADGpdVSGF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 183 MF----NLQEPYFTWpLIAADGGYAfkyengKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGE 256
Cdd:cd14747   157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 257 TAMTINGPWAWSNIDTS----KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK 332
Cdd:cd14747   230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1433048008 333 PLGAvALKSY--EEELAKDPRIAATMENAQKGEIMPNIPQmsafWYAVRTAVINA-----ASGRQTVDEALKDAQT 401
Cdd:cd14747   309 GMLP-ANTSAwdDPSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVleevwIGVGADVEDALDKAAA 379
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 57-350 3.42e-34

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 131.76  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  57 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 132
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 133 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 208
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 209 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 287
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1433048008 288 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 350
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 52-324 4.80e-33

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 128.69  E-value: 4.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  52 YNGLAEVGKKFEKD-TGIKVTVE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPf 127
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 128 twdavrynGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPLIAA 198
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 199 DGGYAFKYENGKYDiKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV- 275
Cdd:pfam01547 158 LGGPLFDKDGGGLD-NPEAVDAITYYVDLYAKVLLLKKLKNPgvAGADGREALALFEQGKAAMGIVGPWAALAANKVKLk 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1433048008 276 ------------NYGVTVLPTFKGQPskpfVGVLSAGINAASPNKELAKEFLeNYLLTDEG 324
Cdd:pfam01547 237 vafaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 62-401 5.02e-32

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 127.88  E-value: 5.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  62 FEKDT-GIKVTVE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQD--KLYPFTWDAVRYNG 136
Cdd:cd14751    23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 137 KLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKYENGky 211
Cdd:cd14751   103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 212 DIKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-----NYGVTVLPT 284
Cdd:cd14751   178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 285 FKGQPSKPfVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDPRIAATMENAQKGE 363
Cdd:cd14751   258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLGLLPTRTSAYEsPEVANNPMVAAFKPALETAV 335

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1433048008 364 IMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT 401
Cdd:cd14751   336 PRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAK 373
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 91-375 5.56e-25

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 107.05  E-value: 5.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  91 GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-PNPPKTWEEI 167
Cdd:cd13655    53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLtEDDVKSLDTM 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 168 paLDKELKAKGKSAlmFNLQEPYFTWPLIAADGGYAFKyeNGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 247
Cdd:cd13655   133 --LAKAPDAKGKVS--FDLSNSWYLYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 248 AEAAFNKGETAMTINGPWAWSNI-DTSKVNYGVTVLPTFK--GQ--PSKPFVGVLSAGINAASPNKELAKEFLEnYLLTD 322
Cdd:cd13655   206 AISGLKDGTLGAGVSGPWDAANLkKALGDNYAVAKLPTYTlgGKdvQMKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNE 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1433048008 323 EGLEAV---NKDKPLGAVALKSyeEELAKDPRIAATMENAQKGEI-MPNIPQMSAFW 375
Cdd:cd13655   285 ESQLTRfekRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
38-379 1.59e-18

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 87.27  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  38 EEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 117
Cdd:COG0687    27 AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVVPSDYFVARLIKAGLLQPLDKS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 118 K--AFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELkaKGKSALmfnLQEPYFTWPL 195
Cdd:COG0687   104 KlpNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL--WDPEY--KGKVAL---LDDPREVLGA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 196 IAADGGYAFkyengkYDIKDVGVDNAGAKagltflvdLIKNKHMNA--DTDYSIAEAAFNKGET--AMTINGPWAWSNID 271
Cdd:COG0687   176 ALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDGAEYIQLLASGEVdlAVGWSGDALALRAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 272 TSKVNYgvtVLPTfKGQPSkpFVGVLSagINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLGAV---ALKSYEEELAK 348
Cdd:COG0687   242 GPPIAY---VIPK-EGALL--WFDNMA--IPKGAPNPDLAYAFI-NFMLSPEVAAALAEYVGYAPPnkaARELLPPELAA 312

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1433048008 349 DPRIAATMENAQKGEIMPNIP-----QMSAFWYAVR 379
Cdd:COG0687   313 NPAIYPPEEVLDKLEFWNPLPpenreLYTRRWTEIK 348
GFP pfam01353
Green fluorescent protein;
431-614 7.26e-15

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 73.76  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 431 LDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 509
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 510 TISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLeyNYNSHNVYITADKQKNGIKANFKIRHNIEDGS- 588
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSL--TGWDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180
                  ....*....|....*....|....*...
gi 1433048008 589 --VQLADHYQQNTPIGDGpVLLPDNHYL 614
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFV 186
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 60-324 5.12e-14

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 73.05  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  60 KKFEKDTGIKVTVEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPDKA------FQDKLYpfTWd 130
Cdd:COG1840     3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPELdaipaeFRDPDG--YW- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 131 avryngkliaYPIAVEALSLIYNKDLLP--NPPKTWEEIpaLDKELKAKgksalmfnlqepyFTWPLIAADG-GYAFkye 207
Cdd:COG1840    79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLL--- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 208 ngkydikdVG--VDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGETAMTINGPWAWSNIDTSKVNYGVtVLPTF 285
Cdd:COG1840   131 --------VAalLQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEV-VFPED 200

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1433048008 286 KGqpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEG 324
Cdd:COG1840   201 GT-----LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 57-320 8.93e-12

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 66.49  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  57 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAVRY 134
Cdd:cd13590    14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 135 NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEiPALDKELkaKGKSAlMFNLQEPYFTWPLIAAdgGYAFkyengkYDIK 214
Cdd:cd13590    94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPAL--KGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 215 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGET--AMTINGPWAWSNIDTSKVNYgvtVLPTFKGQpskp 292
Cdd:cd13590   162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIPKEGGL---- 226

                         250       260
                  ....*....|....*....|....*...
gi 1433048008 293 fVGVLSAGINAASPNKELAKEFLeNYLL 320
Cdd:cd13590   227 -LWVDNMAIPKGAPNPELAHAFI-NFLL 252
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 60-332 3.15e-10

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  60 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPdkaFQDKLYP--------FT 128
Cdd:cd13580    26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 129 WDAVRYNGKLIAYPIAVEALS---LIYNKDLLPN----PPKTWEEipaLDKELKAkgksalmFNLQEP-------YFTWP 194
Cdd:cd13580   103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKA-------FTEKDPdgngkkdTYGLT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 195 LIAADGGYAFK--------YENGKYDIKDVGVDNAG----AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 259
Cdd:cd13580   173 DTKDLIGSGFTglfgafgaPPNNWWKDEDGKLVPGSiqpeMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGI 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 260 TINGPWAWSNIDTSKVNYG----VTVLPTFKGqPSKPFVGVLSAG------INAASPNKELAKEFL------ENYLLTDE 323
Cdd:cd13580   253 FVGNWWDPAWPQASLKKNDpdaeWVAVPIPSG-PDGKYGVWAESGvngffvIPKKSKKPEAILKLLdflsdpEVQKLLDY 331


                  ....*....
gi 1433048008 324 GLEAVNKDK 332
Cdd:cd13580   332 GIEGVHYTV 340
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 56-335 4.61e-10

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 60.70  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  56 AEVGKKFEKDTGIKVTVEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAV 132
Cdd:cd13589    17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 133 RYngkliAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDKELKAK--GKSALmfNLQEPYFTWPLIAADGGyafkyengk 210
Cdd:cd13589    96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGKfpGPRIL--NTSGLALLEAALLADGV--------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 211 yDIKDVGVDNAGAKagltflVDLIKNkhmNADTDY-SIAEAA--FNKGETAMTI--NGPWAWSNIDTSKVNYgvtVLPTf 285
Cdd:cd13589   157 -DPYPLDVDRAFAK------LKELKP---NVVTWWtSGAQLAqlLQSGEVDMAPawNGRAQALIDAGAPVAF---VWPK- 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1433048008 286 kgqpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLG 335
Cdd:cd13589   223 ----EGAILGPDTLAIVKGAPNKELAMKFI-NFALSPEVQAALAEALGYG 267
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 41-329 2.28e-08

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 55.77  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  41 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTVEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 116
Cdd:cd13518     1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 117 DkafQDKLYPFTWDAVryNGKLiaYPIAVEALSLIYNKDLLPNP--PKTWEEIpaLDKELkaKGKSALMFNLQEPYFTWP 194
Cdd:cd13518    77 K---VIEAIPADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKW--KGKIVYPTPLRSGTGLTH 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 195 LIAAdggYAFKYE--NGKYDIKDVGvDNAGAKAGLTFLVDLIKNKHM---NADTDYSIAEAAfnKGETAMTINgpwawsn 269
Cdd:cd13518   146 VAAL---LQLMGEekGGWYLLKLLA-NNGKPVAGNSDAYDLVAKGEVavgLTDTYYAARAAA--KGEPVEIVY------- 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 270 idtskVNYGVTVLPTfkgqpskpfvgvlSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 329
Cdd:cd13518   213 -----PDQGALVIPE-------------GVALLKGAPNPEAAKKFID-FLLSPEGQKALA 253
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 56-160 6.88e-08

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 54.36  E-value: 6.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  56 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVR- 133
Cdd:cd13587    13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1433048008 134 ---YNGKLIAYPIAVEALSLIYNKDLLPNP 160
Cdd:cd13587    93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 50-177 1.78e-07

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 53.07  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  50 KGYnGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYP-F 127
Cdd:cd13588     8 PGY-ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1433048008 128 TW-DAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPAlDKELKAK 177
Cdd:cd13588    87 RNlPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW-DPKYKGR 136
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 58-324 4.12e-07

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 52.84  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  58 VGKKFEKDTGIK-VTVEHPDKL-EEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITPD-------KAFQDKLY 125
Cdd:cd13521    22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKYidqypnlKAFFKQHP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 126 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAK-----GKS-----ALMFNLQ 187
Cdd:cd13521   101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKdpngnGKAdeipfIDRDPLY 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 188 EPYFT---WPLIAADGG--YAFKYENGKydIKDVGVDNAgAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 259
Cdd:cd13521   181 GAFRLinsWGARSAGGStdSDWYEDNGK--FKHPFASEE-YKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKLGG 257

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1433048008 260 TINGPWAWSNIDT---SKVNYGVTVLPTFKGQPSKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDEG 324
Cdd:cd13521   258 FTHNWFASDNLFTaqlGKEKPMYILLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 57-117 3.71e-05

TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 46.20  E-value: 3.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1433048008  57 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 117
Cdd:cd13664    14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKS 74
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 57-328 8.48e-05

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 44.60  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  57 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPdkafqdKLYPFTWDAVR 133
Cdd:cd13545    19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 134 YNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEipaldkelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKYen 208
Cdd:cd13545    93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLL-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 209 gkYDIKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGETAMTI---NGPwAWSNIDTSKVNYGVTVLPTf 285
Cdd:cd13545   152 --WTIAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1433048008 286 kGQpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAV 328
Cdd:cd13545   222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLSPEFQEVI 258
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 61-177 9.42e-05

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 44.73  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  61 KFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFwahdrFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRY----- 134
Cdd:cd13523    18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVT-----PSDSYTSRQLGVGLMQPIDKSLLPSWATLDPHLtlaav 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1433048008 135 ---NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPaLDKELKAK 177
Cdd:cd13523    93 ltvPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL-DDPKYKGR 137
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 92-330 1.51e-04

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 43.89  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  92 PDIIFWAHDRFGG------YAQSGLLAEITPDK-AFQDKLYPFTWdaVRYNGKLIaYPIAVEALSLIYNKDLLPN--PPK 162
Cdd:pfam13343   4 PDIILSAGDLFFDkrflekFIEEGLFQPLDSANlPNVPKDFDDEG--LRDPDGYY-TPYGVGPLVIAYNKERLGGrpVPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 163 TWEEIpaLDKELKakgKSALMFNLqePYFTWPLIAADGGYafkyengkydiKDVGVDnagakAGLTFLVDLIKNKHMNAD 242
Cdd:pfam13343  81 SWADL--LDPEYK---GKVALPGP--NVGDLFNALLLALY-----------KDFGED-----GVRKLARNLKANLHPAQM 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 243 TDYSiaeAAFNKGETAMTInGPWAWSNIDTSKVNYGVTVLPtfkgqPSKPFVGVLSAGINAAspNKELAKEFLeNYLLTD 322
Cdd:pfam13343 138 VKAA---GRLESGEPAVYL-MPYFFADILPRKKKNVEVVWP-----EDGALVSPIFMLVKKG--KKELADPLI-DFLLSP 205


                  ....*...
gi 1433048008 323 EGLEAVNK 330
Cdd:pfam13343 206 EVQAILAK 213
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 60-200 6.11e-04

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 42.37  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  60 KKFEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPDKAfqDKLYPFTWD 130
Cdd:PRK15046   54 PAFTKATGIKVnyveagsgeVVNRAAK-EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKD 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 131 AvryNGKLiaYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELKAKgksalmfnLQepYFTwPLIAADG 200
Cdd:PRK15046  124 A---DGTY--APFVNNYLSFIYNPKVLKTAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDG 175
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 62-323 7.12e-04

Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270266 [Multi-domain]  Cd Length: 310  Bit Score: 42.16  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  62 FEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAHdrfggyaQSGLLAEITPDKAFQDklypftwDAV 132
Cdd:cd13548    21 FTKATGITVnyveagsgeVVERAAK-EKSNPQADVLVTLPPFIQQAA-------QMGLLQPYQSDAAKNP-------AII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 133 RYNGKLIAyPIAVEALSLIYNKDLLPNPPKTWEEI--PALDKEL------KAKGKSALMFNLQEpyftwpLIAADGGYAF 204
Cdd:cd13548    86 KAEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADLldPKYKGKIqystpgQAGDGMAVLLLTTH------LMGSDAAFAY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 205 kyengkydIKDVGVDNAGAKAGLTFLVDLIknkhmnadtdysiaeaafNKGETAMTiNG--PWAWSNIDTSKVNYGVtVL 282
Cdd:cd13548   159 --------LAKLQQNNVGPSASTGKLTALV------------------SKGEISVA-NGdlQMNLAQMEHANPNKKI-FW 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1433048008 283 PTFKGQPSKPFVGVLSAGINAASPNKELAKEfLENYLLTDE 323
Cdd:cd13548   211 PAKAGGQRSTFALPYGIGLVKGAPNADNGKK-LIDFLLSKE 250
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 60-326 8.25e-04

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 42.34  E-value: 8.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  60 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDII--FWaHDRFGGYAQSGLLAEITP--DKA--FQDKLYPFTW-- 129
Cdd:cd13583    24 KEIEEKTNVKFKRTPipSSDYETKRSLLIASGDAPDIIpvLY-PGEENEFVASGALLPISDylDYMpnYKKYVEKWGLgk 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 130 --DAVRY-NGKLIAYPIAVEA----LSLIYNKDLLPN----PPKTWEEIPALDKELKAK-----------GKSALMFNLQ 187
Cdd:cd13583   103 elATGRQsDGKYYSLPGLHEDpgvqYSFLYRKDIFEKagikIPTTWDEFYAALKKLKEKypdsypysdrwNSNALLLIAA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 188 EPYFTWpliaADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMN----ADTDySIAEAAFNKGETAMTING 263
Cdd:cd13583   183 PAFGTT----AGWGFSNYTYDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDpesfTQTD-DQAKAKFLNGKSFVITTN 257

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1433048008 264 PW-----AWSNIDTSKVNYGVTVLPTFKGQ------PSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLE 326
Cdd:cd13583   258 PQtvdelQRNLRAADGGNYEVVSITPPAGPagkainGSRLENGFMISSKAKDSKNFEALLQFL-DWLYSDEGQE 330
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 60-164 9.54e-04

The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270380  Cd Length: 312  Bit Score: 41.73  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  60 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEItpDKAfqdKLYPFTWDAVRYNGKLI 139
Cdd:cd13662    17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKL--DKS---KLPNVKEEKDNLMEASK 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1433048008 140 AY--------PIAVEALSLIYNKDLLPNPPKTW 164
Cdd:cd13662    92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKW 124
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 56-175 1.22e-03

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 41.37  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008  56 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPDKAFQDKLyPFTWDAv 132
Cdd:COG4143    48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1433048008 133 ryNGKLIayPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELK 175
Cdd:COG4143   126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKDK 164
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 106-316 9.05e-03

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270269 [Multi-domain]  Cd Length: 267  Bit Score: 38.54  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 106 AQSGLLAEITPDkaFQDKLypftwDAVRYNGKLIAYPIAVEALSLIYNKDLL--PNPPKTWeeiPALDKElKAKGKSALm 183
Cdd:cd13551    66 KKQGLLVPYTPS--WAGEI-----PSALSDGDGYYYPLVQQPIVLAYNPDTMtdPDAPKSW---TDLAKP-KYKGKYEV- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433048008 184 FNLQEPyfTWPLIAADGGYAFKYENGKYDIKDvgvdnagakAGLTFLVDLIKNKHMNADTDYSIaeAAFNKGETAMTIN- 262
Cdd:cd13551   134 PGLLGG--TGQAILAGILVRYLDPKGEYGVSD---------EGWQVLEDYFANGYPAQEGTDFY--APFADGQVPIGYLw 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1433048008 263 GPWAWSNIDTSKVNYGvtVLPTFKGQpskPFVgVLSAGINAASPNKELAKEFLE 316
Cdd:cd13551   201 SSGLAGIQKQYGVEFK--IVDPEIGV---PFV-TEQVGIVKGTKKEAEAKAFID 248
 
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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