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Conserved domains on  [gi|446618034|ref|WP_000695380|]
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maltose/maltodextrin ABC transporter substrate-binding protein MalE [Escherichia coli]

Protein Classification

maltose/maltodextrin ABC transporter substrate-binding protein( domain architecture ID 11484205)

maltose/maltodextrin ABC transporter substrate-binding protein functions as the primary receptor for the active transport of maltose and higher maltodextrins such as maltotriose

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;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 815.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 241 AAFNKGETAMTINGPWAWSNIDTSKVNYGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446618034 321 KDKPLGAVALKSYQDELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 815.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 241 AAFNKGETAMTINGPWAWSNIDTSKVNYGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446618034 321 KDKPLGAVALKSYQDELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 31-394 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: 683.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  31 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 110
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 111 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 190
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 191 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 270
Cdd:cd13656  161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 271 TILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYQDELAKDPRIAATMDNA 350
Cdd:cd13656  241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446618034 351 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd13656  321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 1.17e-145

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 419.35  E-value: 1.17e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGArILALSALTTMMFSA---------SALAKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKL 69
Cdd:COG2182    1 MKRRLLA-ALALALALALALAAcgsgssssgSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP 149
Cdd:COG2182   79 REKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 150 -NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNK 228
Cdd:COG2182  159 aEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 229 HMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS-KVNYGVTILPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFL 306
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 307 eNYLLTDEGLEAVNKDKPLgAVALKSYQD--ELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 384
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEdaEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 446618034 385 AALKDAQTRITK 396
Cdd:COG2182  395 EALDAAQKQIEA 406
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-341 2.64e-31

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 120.20  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   48 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 123
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  124 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 199
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  200 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTILptfkg 278
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446618034  279 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYQ-DELAKDP 341
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 815.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 241 AAFNKGETAMTINGPWAWSNIDTSKVNYGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446618034 321 KDKPLGAVALKSYQDELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 31-394 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: 683.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  31 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 110
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 111 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 190
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 191 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 270
Cdd:cd13656  161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 271 TILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYQDELAKDPRIAATMDNA 350
Cdd:cd13656  241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446618034 351 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd13656  321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 1.17e-145

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 419.35  E-value: 1.17e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGArILALSALTTMMFSA---------SALAKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKL 69
Cdd:COG2182    1 MKRRLLA-ALALALALALALAAcgsgssssgSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP 149
Cdd:COG2182   79 REKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 150 -NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNK 228
Cdd:COG2182  159 aEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 229 HMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS-KVNYGVTILPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFL 306
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 307 eNYLLTDEGLEAVNKDKPLgAVALKSYQD--ELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 384
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEdaEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 446618034 385 AALKDAQTRITK 396
Cdd:COG2182  395 EALDAAQKQIEA 406
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 32-394 1.43e-143

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: 412.58  E-value: 1.43e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTVEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 107
Cdd:cd13522    1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 108 DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 186
Cdd:cd13522   81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 187 IAADGGYAFKYENGKYDIkdvGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID-TS 264
Cdd:cd13522  161 IGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRqAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 265 KVNYGVTILPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLeaVNKDKPLGAVALKSYQDELAKDPRI 343
Cdd:cd13522  238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446618034 344 A--ATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd13522  316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 32-394 5.36e-132

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: 383.18  E-value: 5.36e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 109
Cdd:cd13586    1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 110 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDK--ELKAKGKSALMFNLQEPYFTWPLI 187
Cdd:cd13586   81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQTNPYFSYPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 188 AADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 266
Cdd:cd13586  161 AAFGGYVFGENGG--DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 267 NYGVTILPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPlGAVALKSYQD--ELAKDPRI 343
Cdd:cd13586  239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTG-RIPALKDALNdaAVKNDPLV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446618034 344 AATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd13586  317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 32-395 6.39e-89

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: 273.20  E-value: 6.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 109
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 110 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 187
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 188 AADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVN 267
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 268 YGVTILPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PlGAVALKSYQDElAKDPRI 343
Cdd:cd13658  241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiP-PRKDVRSDPEI-KNNPLT 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446618034 344 AATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRIT 395
Cdd:cd13658  318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIK 369
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 32-394 5.94e-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: 229.57  E-value: 5.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT- 106
Cdd:cd13657    1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 107 ---PDKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPY 181
Cdd:cd13657   81 ylsEDDF--ENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 182 FTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 261
Cdd:cd13657  159 FVSAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 262 DTSKVNYGVTILPTFKGQ-PSKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYQDELA 338
Cdd:cd13657  233 KAAGIDLGVAPLPTVDGTnPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVA 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446618034 339 KDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd13657  313 ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 32-394 8.02e-56

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: 188.00  E-value: 8.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKGY-NGLAEVGKKFEK-DTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 107
Cdd:cd13585    1 TLTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVVPVpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 108 ---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL------PNPPKTWEEIPALDKELKAKGKS----ALM 174
Cdd:cd13585   81 yieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLEAAKKLTDKKGGqygfALR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 175 FNLQEPYFTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGETAMTI 252
Cdd:cd13585  161 GGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 253 NGPWAWSNIDTSKV--NYGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG---LEAVNKDKPLGA 327
Cdd:cd13585  236 DGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALAA 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446618034 328 VALKSYQDELAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASG--RQTVDAALKDAQTRI 394
Cdd:cd13585  315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-320 1.56e-54

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 184.09  E-value: 1.56e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASALAKIEEGK--LVIWINGDKGYNGLAEVGKKFEKDT-GIKVTVEHP--DKLEEKFPQ 75
Cdd:COG1653    1 MRRLALALAAALALALAACGGGGSGAAAAAGKvtLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  76 VAATGDGPDIIFWAHDRFGGYAQSGLLAEITP----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-- 149
Cdd:COG1653   81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEka 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 150 --NPPKTWEEIPALDKELKAK-GKSALMFNLQEPYFTWPLIAADGGYAFKyENGKydikdVGVDNAGAKAGLTFLVDLIK 226
Cdd:COG1653  161 glDPPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLYD-EDGK-----PAFDSPEAVEALEFLKDLVK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 227 NKHMNAD---TDYSIAEAAFNKGETAMTINGPWAWSNIDTS--KVNYGVTILPTFK-GQPSKPFVGVLSAGINAASPNKE 300
Cdd:COG1653  235 DGYVPPGalgTDWDDARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPE 314

                        330       340
                 ....*....|....*....|
gi 446618034 301 LAKEFLEnYLLTDEGLEAVN 320
Cdd:COG1653  315 AAWKFLK-FLTSPEAQAKWD 333
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 51-394 5.01e-54

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: 183.26  E-value: 5.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  51 KKFEK-DTGIKVTVEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP----DKAFQDKLYPFTWDA 122
Cdd:cd14748   21 DEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyidkDGVDDDDFYPAALDA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 123 VRYNGKLIAYPIAVEALSLIYNKDLL-------PNPPKTWEEI----PALDKELKAKGKSALMFNLQEPYFTW-PLIAAD 190
Cdd:cd14748  101 GTYDGKLYGLPFDTSTPVLYYNKDLFeeagldpEKPPKTWDELeeaaKKLKDKGGKTGRYGFALPPGDGGWTFqALLWQN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 191 GGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI--DTSKVNY 268
Cdd:cd14748  181 GGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIrdKGAGFEY 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 269 GVTILPTFKGQPSKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDEGLEAVNKDK---PLGAVALKSYQDELAKDPRIA 344
Cdd:cd14748  256 GVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylPVRKSAAEDPEEFLAENPNYK 334

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446618034 345 ATMDNAQKG-EIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd14748  335 VAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 41-394 8.06e-39

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: 143.20  E-value: 8.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  41 KGYNGLAEVGKKFEKDT-GIKVTVEH----PDKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITPD-- 108
Cdd:cd14750   11 QEGELLKKAIAAFEKKHpDIKVEIEElpasSDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEYlk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 109 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAKGKSALMFNLQ----EP 180
Cdd:cd14750   87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 181 YFT--WPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGETAMTINGP 255
Cdd:cd14750  167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 256 WAW--SNIDTSKVN--YGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALK 331
Cdd:cd14750  242 YAYalLQGPESAVAgkVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446618034 332 SYQDE--LAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd14750  321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 32-396 1.91e-38

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: 142.13  E-value: 1.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 105
Cdd:cd14749    1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 106 TP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-----NPPKTWEEIPALDKELKAKGK------S 171
Cdd:cd14749   81 TDyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKgqtgfgL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 172 ALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKdvgvDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGET 248
Cdd:cd14749  161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFN----DPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 249 AMTINGPWAWSNIDTSKV--NYGVTILPTFK--GQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKP 324
Cdd:cd14749  236 AMNIGGSWDLGAIKAGEPggKIGVFPFPTVGkgAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQYLEDVG 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446618034 325 LGAVALKSYQDELAKDPRIAATMD--NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRITK 396
Cdd:cd14749  315 LLPAKEVVAKDEDPDPVAILGPFAdvLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 32-396 4.50e-37

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: 138.21  E-value: 4.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTVEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 103
Cdd:cd14747    1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 104 EITP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDKELKAKG--KSAL 173
Cdd:cd14747   77 DLTPyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLkkaggDEAPKTWDELEAAAKKIKADGpdVSGF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 174 MF----NLQEPYFTWpLIAADGGYAfkyengKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGE 247
Cdd:cd14747  157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 248 TAMTINGPWAWSNIDTS----KVNYGVTILPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK 323
Cdd:cd14747  230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 324 PLGAvALKSYQDE--LAKDPRIAATMDNAQKGEIMPNIPQmsafWYAVRTAVINA-----ASGRQTVDAALKDAQTRITK 396
Cdd:cd14747  309 GMLP-ANTSAWDDpsLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVleevwIGVGADVEDALDKAAAEINE 383
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-341 2.64e-31

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 120.20  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   48 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 123
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  124 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 199
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  200 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTILptfkg 278
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446618034  279 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYQ-DELAKDP 341
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 53-394 4.36e-30

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: 119.02  E-value: 4.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  53 FEKDT-GIKVTVE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQD--KLYPFTWDAVRYNG 127
Cdd:cd14751   23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 128 KLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKYENGky 202
Cdd:cd14751  103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 203 DIKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-----NYGVTILPT 275
Cdd:cd14751  178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 276 FKGQPSKPfVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PLGAVALKSyqDELAKDPRIAATMDNAQK 352
Cdd:cd14751  258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLgllPTRTSAYES--PEVANNPMVAAFKPALET 333

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446618034 353 GEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQTRI 394
Cdd:cd14751  334 AVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQW 375
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 43-315 8.04e-30

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: 116.75  E-value: 8.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   43 YNGLAEVGKKFEKD-TGIKVTVE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPf 118
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  119 twdavrynGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPLIAA 189
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  190 DGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNA-DTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-- 266
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVaGADGREALALFEQGKAAMGIVGPWAALAANKVKLkv 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  267 -----------NYGVTILPTFKGQPskpfVGVLSAGINAASPNKELAKEFLeNYLLTDEG 315
Cdd:pfam01547 238 afaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 82-366 2.93e-23

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: 99.73  E-value: 2.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  82 GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-PNPPKTWEEI 158
Cdd:cd13655   53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLtEDDVKSLDTM 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 159 paLDKELKAKGKSAlmFNLQEPYFTWPLIAADGGYAFKyeNGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 238
Cdd:cd13655  133 --LAKAPDAKGKVS--FDLSNSWYLYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 239 AEAAFNKGETAMTINGPWAWSNI-DTSKVNYGVTILPTFK--GQ--PSKPFVGVLSAGINAASPNKELAKEFLEnYLLTD 313
Cdd:cd13655  206 AISGLKDGTLGAGVSGPWDAANLkKALGDNYAVAKLPTYTlgGKdvQMKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNE 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446618034 314 EGLEAV---NKDKPLGAVALKSyqDELAKDPRIAATMDNAQKGEI-MPNIPQMSAFW 366
Cdd:cd13655  285 ESQLTRfekRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-361 5.94e-19

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 87.27  E-value: 5.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASALAkiEEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAA--AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDK--AFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEI 158
Cdd:COG0687   76 SGYDVVVPSDYFVARLIKAGLLQPLDKSKlpNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 159 paLDKELkaKGKSALmfnLQEPYFTWPLIAADGGYAFkyengkYDIKDVGVDNAGAKagltflvdLIKNKHMNA--DTDY 236
Cdd:COG0687  155 --WDPEY--KGKVAL---LDDPREVLGAALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDG 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 237 SIAEAAFNKGET--AMTINGPWAWSNIDTSKVNYGVtilptfkgqPSKPFVGVL-SAGINAASPNKELAKEFLeNYLLTD 313
Cdd:COG0687  214 AEYIQLLASGEVdlAVGWSGDALALRAEGPPIAYVI---------PKEGALLWFdNMAIPKGAPNPDLAYAFI-NFMLSP 283

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446618034 314 EGLEAVNKDKPLGAV---ALKSYQDELAKDPRIAATMDNAQKGEIMPNIPQ 361
Cdd:COG0687  284 EVAAALAEYVGYAPPnkaARELLPPELAANPAIYPPEEVLDKLEFWNPLPP 334
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 51-315 8.11e-12

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 65.34  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  51 KKFEKDTGIKVTVEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPDKA------FQDKLYpfTWd 121
Cdd:COG1840    3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPELdaipaeFRDPDG--YW- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 122 avryngkliaYPIAVEALSLIYNKDLLP--NPPKTWEEIpaLDKELKAKgksalmfnlqepyFTWPLIAADG-GYAFkye 198
Cdd:COG1840   79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLL--- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 199 ngkydikdVG--VDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGETAMTINGPWAWSNIDTSKVNYGVtILPTF 276
Cdd:COG1840  131 --------VAalLQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEV-VFPED 200

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446618034 277 KGqpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEG 315
Cdd:COG1840  201 GT-----LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-361 1.74e-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: 62.34  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  51 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPdkaFQDKLYP--------FT 119
Cdd:cd13580   26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 120 WDAVRYNGKLIAYPIAVEALS---LIYNKDLLPN----PPKTWEEipaLDKELKAkgksalmFNLQEP-------YFTWP 185
Cdd:cd13580  103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKA-------FTEKDPdgngkkdTYGLT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 186 LIAADGGYAFK--------YENGKYDIKDVGVDNAG----AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 250
Cdd:cd13580  173 DTKDLIGSGFTglfgafgaPPNNWWKDEDGKLVPGSiqpeMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGI 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 251 TINGPWAWSNIDTSKVNYG----VTILPTFKGqPSKPFVGVLSAG------INAASPNKELAKEFL------ENYLLTDE 314
Cdd:cd13580  253 FVGNWWDPAWPQASLKKNDpdaeWVAVPIPSG-PDGKYGVWAESGvngffvIPKKSKKPEAILKLLdflsdpEVQKLLDY 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 446618034 315 GLEAVN-KDKPLGAVALKSYQDELAKDPRIAA--TMDNAQKGEIMPNIPQ 361
Cdd:cd13580  332 GIEGVHyTVKDGGPVNIIPPDKQEVGDATLDYfqGSLALEKYKLTNNGER 381
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 48-311 2.36e-10

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: 61.10  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  48 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAVRY 125
Cdd:cd13590   14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 126 NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEiPALDKELkaKGKSAlMFNLQEPYFTWPLIAAdgGYAFkyengkYDIK 205
Cdd:cd13590   94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPAL--KGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 206 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGET--AMTINGPWAWSNIDTSKVNYgvtILPTFKGQpskp 283
Cdd:cd13590  162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIPKEGGL---- 226

                        250       260
                 ....*....|....*....|....*...
gi 446618034 284 fVGVLSAGINAASPNKELAKEFLeNYLL 311
Cdd:cd13590  227 -LWVDNMAIPKGAPNPELAHAFI-NFLL 252
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 47-326 4.23e-08

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: 53.77  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  47 AEVGKKFEKDTGIKVTVEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAV 123
Cdd:cd13589   17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 124 RYngkliAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDKELKAK--GKSALmfNLQEPYFTWPLIAADGGyafkyengk 201
Cdd:cd13589   96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGKfpGPRIL--NTSGLALLEAALLADGV--------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 202 yDIKDVGVDNAGAKagltflVDLIKNkhmNADTDY-SIAEAA--FNKGETAMtinGPWAWSNIDTSKVNyGVTILPTFKG 278
Cdd:cd13589  157 -DPYPLDVDRAFAK------LKELKP---NVVTWWtSGAQLAqlLQSGEVDM---APAWNGRAQALIDA-GAPVAFVWPK 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446618034 279 qpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLG 326
Cdd:cd13589  223 --EGAILGPDTLAIVKGAPNKELAMKFI-NFALSPEVQAALAEALGYG 267
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 47-151 1.38e-07

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: 52.44  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  47 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVR- 124
Cdd:cd13587   13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 446618034 125 ---YNGKLIAYPIAVEALSLIYNKDLLPNP 151
Cdd:cd13587   93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 41-168 5.39e-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: 50.76  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  41 KGYnGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYP-F 118
Cdd:cd13588    8 PGY-ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446618034 119 TW-DAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPAlDKELKAK 168
Cdd:cd13588   87 RNlPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW-DPKYKGR 136
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 49-315 7.95e-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: 50.92  E-value: 7.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  49 VGKKFEKDTGIK-VTVEHPDKL-EEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITPD-------KAFQDKLY 116
Cdd:cd13521   22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKYidqypnlKAFFKQHP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 117 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAK-----GKS-----ALMFNLQ 178
Cdd:cd13521  101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKdpngnGKAdeipfIDRDPLY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 179 EPYFT---WPLIAADGG--YAFKYENGKydIKDVGVDNAgAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 250
Cdd:cd13521  181 GAFRLinsWGARSAGGStdSDWYEDNGK--FKHPFASEE-YKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKLGG 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446618034 251 TINGPWAWSNIDT---SKVNYGVTILPTFKGQPSKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDEG 315
Cdd:cd13521  258 FTHNWFASDNLFTaqlGKEKPMYILLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 32-320 9.41e-07

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: 49.61  E-value: 9.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  32 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTVEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 107
Cdd:cd13518    1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 108 DkafQDKLYPFTWDAVryNGKLiaYPIAVEALSLIYNKDLLPNP--PKTWEEIpaLDKELkaKGKSALMFNLQEPYFTWP 185
Cdd:cd13518   77 K---VIEAIPADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKW--KGKIVYPTPLRSGTGLTH 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 186 LIAAdggYAFKYE--NGKYDIKDVGvDNAGAKAGLTFLVDLIKNKHM---NADTDYSIAEAAfnKGETAMTINgpwawsn 260
Cdd:cd13518  146 VAAL---LQLMGEekGGWYLLKLLA-NNGKPVAGNSDAYDLVAKGEVavgLTDTYYAARAAA--KGEPVEIVY------- 212

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 261 idtskVNYGVTILPTfkgqpskpfvgvlSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 320
Cdd:cd13518  213 -----PDQGALVIPE-------------GVALLKGAPNPEAAKKFID-FLLSPEGQKALA 253
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 48-108 3.37e-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: 45.43  E-value: 3.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446618034  48 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 108
Cdd:cd13664   14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKS 74
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 48-319 6.91e-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: 44.21  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  48 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPdkafqdKLYPFTWDAVR 124
Cdd:cd13545   19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 125 YNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEipaldkelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKYen 199
Cdd:cd13545   93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLL-- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 200 gkYDIKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGETAMTI---NGPwAWSNIDTSKVNYGVTILPTf 276
Cdd:cd13545  152 --WTIAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446618034 277 kGQpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAV 319
Cdd:cd13545  222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLSPEFQEVI 258
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 52-168 2.02e-04

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: 42.81  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  52 KFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFwahdrFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRY----- 125
Cdd:cd13523   18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVT-----PSDSYTSRQLGVGLMQPIDKSLLPSWATLDPHLtlaav 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446618034 126 ---NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPaLDKELKAK 168
Cdd:cd13523   93 ltvPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL-DDPKYKGR 137
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-317 4.34e-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: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  51 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDII--FWaHDRFGGYAQSGLLAEITP--DKA--FQDKLYPFTW-- 120
Cdd:cd13583   24 KEIEEKTNVKFKRTPipSSDYETKRSLLIASGDAPDIIpvLY-PGEENEFVASGALLPISDylDYMpnYKKYVEKWGLgk 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 121 --DAVRY-NGKLIAYPIAVEA----LSLIYNKDLLPN----PPKTWEEIPALDKELKAK-----------GKSALMFNLQ 178
Cdd:cd13583  103 elATGRQsDGKYYSLPGLHEDpgvqYSFLYRKDIFEKagikIPTTWDEFYAALKKLKEKypdsypysdrwNSNALLLIAA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 179 EPYFTWpliaADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMN----ADTDySIAEAAFNKGETAMTING 254
Cdd:cd13583  183 PAFGTT----AGWGFSNYTYDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDpesfTQTD-DQAKAKFLNGKSFVITTN 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446618034 255 PW-----AWSNIDTSKVNYGVTILPTFKGQ------PSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLE 317
Cdd:cd13583  258 PQtvdelQRNLRAADGGNYEVVSITPPAGPagkainGSRLENGFMISSKAKDSKNFEALLQFL-DWLYSDEGQE 330
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 51-155 5.51e-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: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  51 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEItpDKAfqdKLYPFTWDAVRYNGKLI 130
Cdd:cd13662   17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKL--DKS---KLPNVKEEKDNLMEASK 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446618034 131 AY--------PIAVEALSLIYNKDLLPNPPKTW 155
Cdd:cd13662   92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKW 124
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 1-191 6.12e-04

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 41.60  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   1 MKIKTGARILALSALTTMMFSASAL---AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKV---------TVEHPDK 68
Cdd:PRK15046   1 MRSTNRAAAAAAMKLAAAAAAAAFGggaAPAWAADAVTVYSADGLEDWYQDVFPAFTKATGIKVnyveagsgeVVNRAAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  69 lEEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPDKAfqDKLYPFTWDAvryNGKLiaYPIAVEALSLIYNKDLL 148
Cdd:PRK15046  81 -EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKDA---DGTY--APFVNNYLSFIYNPKVL 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446618034 149 PNPPKTWEEIpaLDKELKAKgksalmfnLQepYFTwPLIAADG 191
Cdd:PRK15046 146 KTAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDG 175
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 47-166 1.80e-03

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 40.22  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  47 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPDKAFQDKLyPFTWDAv 123
Cdd:COG4143   48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446618034 124 ryNGKLIayPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELK 166
Cdd:COG4143  126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKDK 164
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 83-321 2.76e-03

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 39.26  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034   83 PDIIFWAHDRFGG------YAQSGLLAEITPDK-AFQDKLYPFTWdaVRYNGKLIaYPIAVEALSLIYNKDLLPN--PPK 153
Cdd:pfam13343   4 PDIILSAGDLFFDkrflekFIEEGLFQPLDSANlPNVPKDFDDEG--LRDPDGYY-TPYGVGPLVIAYNKERLGGrpVPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  154 TWEEIpaLDKELKakgKSALMFNLqePYFTWPLIAADGGYafkyengkydiKDVGVDnagakAGLTFLVDLIKNKHMNAD 233
Cdd:pfam13343  81 SWADL--LDPEYK---GKVALPGP--NVGDLFNALLLALY-----------KDFGED-----GVRKLARNLKANLHPAQM 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  234 TDYSiaeAAFNKGETAMTInGPWAWSNIDTSKVNYGVTILPtfkgqPSKPFVGVLSAGINAAspNKELAKEFLeNYLLTD 313
Cdd:pfam13343 138 VKAA---GRLESGEPAVYL-MPYFFADILPRKKKNVEVVWP-----EDGALVSPIFMLVKKG--KKELADPLI-DFLLSP 205


                  ....*...
gi 446618034  314 EGLEAVNK 321
Cdd:pfam13343 206 EVQAILAK 213
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 53-314 4.36e-03

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: 38.70  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034  53 FEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAHdrfggyaQSGLLAEITPDKAFQDklypftwDAV 123
Cdd:cd13548   21 FTKATGITVnyveagsgeVVERAAK-EKSNPQADVLVTLPPFIQQAA-------QMGLLQPYQSDAAKNP-------AII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 124 RYNGKLIAyPIAVEALSLIYNKDLLPNPPKTWEEI--PALDKEL------KAKGKSALMFNLQEpyftwpLIAADGGYAF 195
Cdd:cd13548   86 KAEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADLldPKYKGKIqystpgQAGDGMAVLLLTTH------LMGSDAAFAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446618034 196 kyengkydIKDVGVDNAGAKAGLTFLVDLIknkhmnadtdysiaeaafNKGETAMTiNG--PWAWSNIDTSKVNYGVtIL 273
Cdd:cd13548  159 --------LAKLQQNNVGPSASTGKLTALV------------------SKGEISVA-NGdlQMNLAQMEHANPNKKI-FW 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446618034 274 PTFKGQPSKPFVGVLSAGINAASPNKELAKEfLENYLLTDE 314
Cdd:cd13548  211 PAKAGGQRSTFALPYGIGLVKGAPNADNGKK-LIDFLLSKE 250
 
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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