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Conserved domains on  [gi|323462859|pdb|3LC8|A]
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Chain A, Maltose-binding periplasmic protein, Renin receptor

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;
3-366 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 776.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         3 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 82
Cdd:PRK09474  29 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        83 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPLIA 162
Cdd:PRK09474 109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       163 ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY 242
Cdd:PRK09474 189 ADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINY 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       243 GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME 322
Cdd:PRK09474 269 GVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAATMD 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
3LC8_A       323 NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:PRK09474 349 NAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAK 392
Renin_r super family cl06748
Renin receptor-like protein; The sequences featured in this family are similar to a region of ...
 366-384 9.19e-09

Renin receptor-like protein; The sequences featured in this family are similar to a region of the human renin receptor that bears a putative transmembrane spanning segment. The renin receptor is involved in intracellular signal transduction by the activation of the ERK1/ERK2 pathway, and it also serves to increase the efficiency of angiotensinogen cleavage by receptor-bound renin, therefore facilitating angiotensin II generation and action on a cell surface.


The actual alignment was detected with superfamily member pfam07850:

Pssm-ID: 462287  Cd Length: 97  Bit Score: 52.31  E-value: 9.19e-09
                          10
                  ....*....|....*....
3LC8_A        366 DPGYDSIIYRMTNQKIRMD 384
Cdd:pfam07850  79 DPGRDSIIYRMTTTRMKKD 97
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
3-366 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 776.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         3 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 82
Cdd:PRK09474  29 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        83 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPLIA 162
Cdd:PRK09474 109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       163 ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY 242
Cdd:PRK09474 189 ADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINY 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       243 GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME 322
Cdd:PRK09474 269 GVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAATMD 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
3LC8_A       323 NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:PRK09474 349 NAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAK 392
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 5-365 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: 680.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        5 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 84
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       85 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPLIAAD 164
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      165 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 244
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      245 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 324
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
3LC8_A      325 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAA 365
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 361
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-366 1.45e-142

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 410.88  E-value: 1.45e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        1 ETEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAE 78
Cdd:COG2182  35 AGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAP 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       79 ITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDRELKAKGKSALMFNLQEPYFT 157
Cdd:COG2182 114 LDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYF 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      158 WPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT 237
Cdd:COG2182 194 YPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKK 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      238 S-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAK 313
Cdd:COG2182 272 AlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKA 349

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
3LC8_A      314 DPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:COG2182 350 DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQK 402
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 22-315 2.40e-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: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         22 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 97
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         98 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIpaLDRELKAKGKsalmfnlqepyFTWPLIAADGGYAFKYEN 173
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDEL--LAAAAKLKGK-----------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        174 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 252
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
3LC8_A        253 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 315
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
Renin_r pfam07850
Renin receptor-like protein; The sequences featured in this family are similar to a region of ...
 366-384 9.19e-09

Renin receptor-like protein; The sequences featured in this family are similar to a region of the human renin receptor that bears a putative transmembrane spanning segment. The renin receptor is involved in intracellular signal transduction by the activation of the ERK1/ERK2 pathway, and it also serves to increase the efficiency of angiotensinogen cleavage by receptor-bound renin, therefore facilitating angiotensin II generation and action on a cell surface.


Pssm-ID: 462287  Cd Length: 97  Bit Score: 52.31  E-value: 9.19e-09
                          10
                  ....*....|....*....
3LC8_A        366 DPGYDSIIYRMTNQKIRMD 384
Cdd:pfam07850  79 DPGRDSIIYRMTTTRMKKD 97
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
3-366 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 776.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         3 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 82
Cdd:PRK09474  29 EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        83 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPLIA 162
Cdd:PRK09474 109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       163 ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY 242
Cdd:PRK09474 189 ADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSGINY 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       243 GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME 322
Cdd:PRK09474 269 GVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAATMD 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
3LC8_A       323 NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:PRK09474 349 NAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAK 392
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 5-365 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: 680.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        5 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 84
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       85 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPLIAAD 164
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      165 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 244
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      245 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 324
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
3LC8_A      325 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAA 365
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 361
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-366 1.45e-142

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 410.88  E-value: 1.45e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        1 ETEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAE 78
Cdd:COG2182  35 AGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAP 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       79 ITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDRELKAKGKSALMFNLQEPYFT 157
Cdd:COG2182 114 LDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYF 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      158 WPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT 237
Cdd:COG2182 194 YPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKK 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      238 S-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAK 313
Cdd:COG2182 272 AlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKA 349

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
3LC8_A      314 DPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:COG2182 350 DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQK 402
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 6-364 1.57e-142

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: 409.49  E-value: 1.57e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTVEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 81
Cdd:cd13522   1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       82 DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDRELKAKGKSALMFNLQEPYFTWPL 160
Cdd:cd13522  81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      161 IAADGGYAFKYENGKYDIkdvGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID-TS 238
Cdd:cd13522 161 IGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRqAL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      239 KVNYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLeaVNKDKPLGAVALKSYEEELAKDPRI 317
Cdd:cd13522 238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
3LC8_A      318 A--ATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 364
Cdd:cd13522 316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDA 364
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 6-364 1.20e-131

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: 381.64  E-value: 1.20e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 83
Cdd:cd13586   1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       84 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPAL--DRELKAKGKSALMFNLQEPYFTWPLI 161
Cdd:cd13586  81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALakKFNDKAGGKYGFAYDQTNPYFSYPFL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      162 AADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 240
Cdd:cd13586 161 AAFGGYVFGENGG--DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      241 NYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPlGAVALKSYEE--ELAKDPRI 317
Cdd:cd13586 239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTG-RIPALKDALNdaAVKNDPLV 316

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
3LC8_A      318 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 364
Cdd:cd13586 317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDA 363
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 6-364 2.31e-87

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


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 268.97  E-value: 2.31e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 83
Cdd:cd13658   1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       84 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDREL--KAKGKSALMFNLQEPYFTWPLI 161
Cdd:cd13658  81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      162 AADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVN 241
Cdd:cd13658 161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      242 YGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PlGAVALKSYEEElAKDPRI 317
Cdd:cd13658 241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiP-PRKDVRSDPEI-KNNPLT 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
3LC8_A      318 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 364
Cdd:cd13658 318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDA 364
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 6-365 5.15e-71

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: 226.87  E-value: 5.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT- 80
Cdd:cd13657   1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       81 ---PDKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDREL--KAKGKSALMFNLQEPY 155
Cdd:cd13657  81 ylsEDDF--ENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      156 FTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 235
Cdd:cd13657 159 FVSAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGI 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      236 DTSKVNYGVTVLPTFKGQ-PSKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELA 312
Cdd:cd13657 233 KAAGIDLGVAPLPTVDGTnPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVA 312

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
3LC8_A      313 KDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAA 365
Cdd:cd13657 313 ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 6-366 6.10e-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: 6.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKGY-NGLAEVGKKFEK-DTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 81
Cdd:cd13585   1 TLTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVVPVpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       82 ---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL------PNPPKTWEEIPALDRELKAKGKS----ALM 148
Cdd:cd13585  81 yieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLEAAKKLTDKKGGqygfALR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      149 FNLQEPYFTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGETAMTI 226
Cdd:cd13585 161 GGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMMI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      227 NGPWAWSNIDTSKV--NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG---LEAVNKDKPLGA 301
Cdd:cd13585 236 DGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALAA 314

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3LC8_A      302 VALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASG--RQTVDEALKDAAD 366
Cdd:cd13585 315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAK 381
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 25-366 2.91e-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: 183.65  E-value: 2.91e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       25 KKFEK-DTGIKVTVEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP----DKAFQDKLYPFTWDA 96
Cdd:cd14748  21 DEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyidkDGVDDDDFYPAALDA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       97 VRYNGKLIAYPIAVEALSLIYNKDLL-------PNPPKTWEEI----PALDRELKAKGKSALMFNLQEPYFTW-PLIAAD 164
Cdd:cd14748 101 GTYDGKLYGLPFDTSTPVLYYNKDLFeeagldpEKPPKTWDELeeaaKKLKDKGGKTGRYGFALPPGDGGWTFqALLWQN 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      165 GGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI--DTSKVNY 242
Cdd:cd14748 181 GGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIrdKGAGFEY 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      243 GVTVLPTFKGQPSKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDEGLEAVNKDK---PLGAVALKSYEEELAKDPRIA 318
Cdd:cd14748 256 GVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylPVRKSAAEDPEEFLAENPNYK 334

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
3LC8_A      319 ATMENAQKG-EIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:cd14748 335 VAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 3-294 1.95e-53

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 181.01  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        3 EEGKLVIWINGDKGYNGLAEVGKKFEKDT-GIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 79
Cdd:COG1653  31 GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       80 TP----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDRELKAK-GKSALMFN 150
Cdd:COG1653 111 DDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEkaglDPPKTWDELLAAAKKLKAKdGVYGFALG 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      151 LQEPYFTWPLIAADGGYAFKyENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAMTIN 227
Cdd:COG1653 191 GKDGAAWLDLLLSAGGDLYD-EDGK-----PAFDSPEAVEALEFLKDLVKDGYVPPGalgTDWDDARAAFASGKAAMMIN 264

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      228 GPWAWSNIDTS--KVNYGVTVLPTFK-GQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 294
Cdd:COG1653 265 GSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKWD 333
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 15-366 4.63e-38

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: 140.89  E-value: 4.63e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       15 KGYNGLAEVGKKFEKDT-GIKVTVEH----PDKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITPD-- 82
Cdd:cd14750  11 QEGELLKKAIAAFEKKHpDIKVEIEElpasSDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEYlk 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       83 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDRELKAKGKSALMFNLQ----EP 154
Cdd:cd14750  87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      155 YFT--WPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGETAMTINGP 229
Cdd:cd14750 167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      230 WAW--SNIDTSKVN--YGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALK 305
Cdd:cd14750 242 YAYalLQGPESAVAgkVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3LC8_A      306 SYEEE--LAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:cd14750 321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQE 383
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 6-366 2.23e-37

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: 139.05  E-value: 2.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 79
Cdd:cd14749   1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       80 TP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-----NPPKTWEEIPALDRELKAKGK------S 145
Cdd:cd14749  81 TDyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKgqtgfgL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      146 ALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKdvgvDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGET 222
Cdd:cd14749 161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFN----DPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      223 AMTINGPWAWSNIDTSKV--NYGVTVLPTFK--GQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEA-VNKDK 297
Cdd:cd14749 236 AMNIGGSWDLGAIKAGEPggKIGVFPFPTVGkgAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQyLEDVG 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      298 PLGAVALKSYEEELAKDPRIAATME-NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:cd14749 315 LLPAKEVVAKDEDPDPVAILGPFADvLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQS 384
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 6-366 2.47e-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: 138.99  E-value: 2.47e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTVEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 77
Cdd:cd14747   1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       78 EITP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDRELKAKG--KSAL 147
Cdd:cd14747  77 DLTPyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLkkaggDEAPKTWDELEAAAKKIKADGpdVSGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      148 MF----NLQEPYFTWpLIAADGGYAfkyengKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGE 221
Cdd:cd14747 157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      222 TAMTINGPWAWSNIDTS----KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK 297
Cdd:cd14747 230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3LC8_A      298 PLGAvALKSY--EEELAKDPRIAATMENAQKGEIMPNIPQmsafWYAVRTAVINA-----ASGRQTVDEALKDAAD 366
Cdd:cd14747 309 GMLP-ANTSAwdDPSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVleevwIGVGADVEDALDKAAA 379
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 27-366 8.03e-32

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


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 123.64  E-value: 8.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       27 FEKDT-GIKVTVE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQD--KLYPFTWDAVRYNG 101
Cdd:cd14751  23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      102 KLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDRE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKYENGky 176
Cdd:cd14751 103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      177 DIKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-----NYGVTVLPT 249
Cdd:cd14751 178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      250 FKGQPSKPfVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDPRIAATMENAQKGE 328
Cdd:cd14751 258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLGLLPTRTSAYEsPEVANNPMVAAFKPALETAV 335

                       330       340       350
                ....*....|....*....|....*....|....*...
3LC8_A      329 IMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAAD 366
Cdd:cd14751 336 PRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAK 373
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 22-315 2.40e-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: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         22 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 97
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         98 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIpaLDRELKAKGKsalmfnlqepyFTWPLIAADGGYAFKYEN 173
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDEL--LAAAAKLKGK-----------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        174 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 252
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
3LC8_A        253 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 315
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 17-289 5.47e-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: 5.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         17 YNGLAEVGKKFEKD-TGIKVTVE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPf 92
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         93 twdavrynGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDRELKAKGKSALMFNLQEP-----YFTWPLIAA 163
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        164 DGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNA-DTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-- 240
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVaGADGREALALFEQGKAAMGIVGPWAALAANKVKLkv 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        241 -----------NYGVTVLPTFKGQPskpfVGVLSAGINAASPNKELAKEFLeNYLLTDEG 289
Cdd:pfam01547 238 afaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 56-340 5.27e-24

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: 101.65  E-value: 5.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       56 GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-PNPPKTWEEI 132
Cdd:cd13655  53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLtEDDVKSLDTM 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      133 PALDRELKAKgksaLMFNLQEPYFTWPLIAADGGYAFKyeNGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 212
Cdd:cd13655 133 LAKAPDAKGK----VSFDLSNSWYLYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      213 AEAAFNKGETAMTINGPWAWSNI-DTSKVNYGVTVLPTFK--GQ--PSKPFVGVLSAGINAASPNKELAKEFLEnYLLTD 287
Cdd:cd13655 206 AISGLKDGTLGAGVSGPWDAANLkKALGDNYAVAKLPTYTlgGKdvQMKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNE 284

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
3LC8_A      288 EGLEAV---NKDKPLGAVALKSyeEELAKDPRIAATMENAQKGEI-MPNIPQMSAFW 340
Cdd:cd13655 285 ESQLTRfekRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
3-335 2.51e-16

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 79.18  E-value: 2.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        3 EEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 82
Cdd:COG0687  27 AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVVPSDYFVARLIKAGLLQPLDKS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       83 K--AFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDRELkaKGKSALmfnLQEPYFTWPL 160
Cdd:COG0687 104 KlpNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL--WDPEY--KGKVAL---LDDPREVLGA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      161 IAADGGYAFkyengkYDIKDVGVDNAGAKagltflvdLIKNKHMNA--DTDYSIAEAAFNKGET--AMTINGPWAWSNID 236
Cdd:COG0687 176 ALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDGAEYIQLLASGEVdlAVGWSGDALALRAE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      237 TSKVNYgvtVLPTfkgqpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLGAV---ALKSYEEELAK 313
Cdd:COG0687 242 GPPIAY---VIPK-----EGALLWFDNMAIPKGAPNPDLAYAFI-NFMLSPEVAAALAEYVGYAPPnkaARELLPPELAA 312

                       330       340
                ....*....|....*....|..
3LC8_A      314 DPRIAATMENAQKGEIMPNIPQ 335
Cdd:COG0687 313 NPAIYPPEEVLDKLEFWNPLPP 334
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 25-289 3.92e-12

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 66.11  E-value: 3.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       25 KKFEKDTGIKVTVEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPDKA------FQDKLYpfTWd 95
Cdd:COG1840   3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPELdaipaeFRDPDG--YW- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       96 avryngkliaYPIAVEALSLIYNKDLLP--NPPKTWEEIpaLDRELKAKgksalmfnlqepyFTWPLIAADG-GYAFkye 172
Cdd:COG1840  79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLL--- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      173 ngkydikdVG--VDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGETAMTINGPWAWSNIDTSKVNYGVtVLPTF 250
Cdd:COG1840 131 --------VAalLQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEV-VFPED 200

                       250       260       270
                ....*....|....*....|....*....|....*....
3LC8_A      251 KGqpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEG 289
Cdd:COG1840 201 GT-----LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 22-285 1.22e-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: 61.87  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       22 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAVRY 99
Cdd:cd13590  14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      100 NGKLIAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDRELKAKGKSAlMFNLQEPYFTWPLIAAdgGYAFkyengkYDIK 179
Cdd:cd13590  94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSW---DLDLWDPALKGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      180 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGET--AMTINGPWAWSNIDTSKVNYgvtVLPTFKGQpskp 257
Cdd:cd13590 162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIPKEGGL---- 226

                       250       260
                ....*....|....*....|....*...
3LC8_A      258 fVGVLSAGINAASPNKELAKEFLeNYLL 285
Cdd:cd13590 227 -LWVDNMAIPKGAPNPELAHAFI-NFLL 252
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 25-297 4.11e-09

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: 58.11  E-value: 4.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       25 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPdkaFQDKLYP--------FT 93
Cdd:cd13580  26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       94 WDAVRYNGKLIAYPIAVEALS---LIYNKDLLPN----PPKTWEEipaLDRELKAkgksalmFNLQEP-------YFTWP 159
Cdd:cd13580 103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKA-------FTEKDPdgngkkdTYGLT 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      160 LIAADGGYAFK--------YENGKYDIKDVGVDNAG----AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 224
Cdd:cd13580 173 DTKDLIGSGFTglfgafgaPPNNWWKDEDGKLVPGSiqpeMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGI 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      225 TINGPWAWSNIDTSKVNYG----VTVLPTFKGqPSKPFVGVLSAG------INAASPNKELAKEFL------ENYLLTDE 288
Cdd:cd13580 253 FVGNWWDPAWPQASLKKNDpdaeWVAVPIPSG-PDGKYGVWAESGvngffvIPKKSKKPEAILKLLdflsdpEVQKLLDY 331


                ....*....
3LC8_A      289 GLEAVNKDK 297
Cdd:cd13580 332 GIEGVHYTV 340
Renin_r pfam07850
Renin receptor-like protein; The sequences featured in this family are similar to a region of ...
 366-384 9.19e-09

Renin receptor-like protein; The sequences featured in this family are similar to a region of the human renin receptor that bears a putative transmembrane spanning segment. The renin receptor is involved in intracellular signal transduction by the activation of the ERK1/ERK2 pathway, and it also serves to increase the efficiency of angiotensinogen cleavage by receptor-bound renin, therefore facilitating angiotensin II generation and action on a cell surface.


Pssm-ID: 462287  Cd Length: 97  Bit Score: 52.31  E-value: 9.19e-09
                          10
                  ....*....|....*....
3LC8_A        366 DPGYDSIIYRMTNQKIRMD 384
Cdd:pfam07850  79 DPGRDSIIYRMTTTRMKKD 97
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 21-300 2.73e-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: 54.54  E-value: 2.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       21 AEVGKKFEKDTGIKVTVEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAV 97
Cdd:cd13589  17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       98 RYngkliAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDRELKAK--GKSALmfNLQEPYFTWPLIAADGGyafkyengk 175
Cdd:cd13589  96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGKfpGPRIL--NTSGLALLEAALLADGV--------- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      176 yDIKDVGVDNAGAKagltflVDLIKNkhmNADTDY-SIAEAA--FNKGETAMTI--NGPWAWSNIDTSKVNYgvtVLPTf 250
Cdd:cd13589 157 -DPYPLDVDRAFAK------LKELKP---NVVTWWtSGAQLAqlLQSGEVDMAPawNGRAQALIDAGAPVAF---VWPK- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
3LC8_A      251 kgqpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLG 300
Cdd:cd13589 223 ----EGAILGPDTLAIVKGAPNKELAMKFI-NFALSPEVQAALAEALGYG 267
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 21-125 1.16e-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: 52.82  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       21 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVR- 98
Cdd:cd13587  13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                        90       100       110
                ....*....|....*....|....*....|
3LC8_A       99 ---YNGKLIAYPIAVEALSLIYNKDLLPNP 125
Cdd:cd13587  93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 6-294 6.81e-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: 49.99  E-value: 6.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        6 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTVEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 81
Cdd:cd13518   1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       82 DkafQDKLYPFTWDAVryNGKLiaYPIAVEALSLIYNKDLLPNP--PKTWEEIpaLDRELkaKGKSALMFNLQEPYFTWP 159
Cdd:cd13518  77 K---VIEAIPADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKW--KGKIVYPTPLRSGTGLTH 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      160 LIAAdggYAFKYE--NGKYDIKDVGvDNAGAKAGLTFLVDLIKNKHM---NADTDYSIAEAAfnKGETAMTINgpwawsn 234
Cdd:cd13518 146 VAAL---LQLMGEekGGWYLLKLLA-NNGKPVAGNSDAYDLVAKGEVavgLTDTYYAARAAA--KGEPVEIVY------- 212

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      235 idtskVNYGVTVLPTfkgqpskpfvgvlSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 294
Cdd:cd13518 213 -----PDQGALVIPE-------------GVALLKGAPNPEAAKKFID-FLLSPEGQKALA 253
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 25-129 9.33e-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: 49.99  E-value: 9.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       25 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYP-FTW-DAVRYNG 101
Cdd:cd13588  17 TAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrLRNlPWLTVDG 96

                        90       100
                ....*....|....*....|....*...
3LC8_A      102 KLIAYPIAVEALSLIYNKDLLPNPPKTW 129
Cdd:cd13588  97 KVYGVPYDWGANGLAYNTKKVKTPPTSW 124
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 23-289 9.63e-06

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: 47.45  E-value: 9.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       23 VGKKFEKDTGIK-VTVEHPDKL-EEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITPD-------KAFQDKLY 90
Cdd:cd13521  22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKYidqypnlKAFFKQHP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       91 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLLPN----PPKTWEEIPALDRELKAK-----GKS-----ALMFNLQ 152
Cdd:cd13521 101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKdpngnGKAdeipfIDRDPLY 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      153 EPYFT---WPLIAADGG--YAFKYENGKydIKDVGVDNAgAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 224
Cdd:cd13521 181 GAFRLinsWGARSAGGStdSDWYEDNGK--FKHPFASEE-YKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKLGG 257

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3LC8_A      225 TINGPWAWSNIDT---SKVNYGVTVLPTFKGQPSKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDEG 289
Cdd:cd13521 258 FTHNWFASDNLFTaqlGKEKPMYILLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 22-82 3.63e-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: 45.04  E-value: 3.63e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3LC8_A       22 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 82
Cdd:cd13664  14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKS 74
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 22-293 2.02e-04

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: 42.67  E-value: 2.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       22 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPdkafqdKLYPFTWDAVR 98
Cdd:cd13545  19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       99 YNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEipaldrelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKYen 173
Cdd:cd13545  93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLL-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      174 gkYDIKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGETAMTI---NGPwAWSNIDTSKVNYGVTVLPTf 250
Cdd:cd13545 152 --WTIAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
3LC8_A      251 kGQpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAV 293
Cdd:cd13545 222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLSPEFQEVI 258
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 25-153 2.55e-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: 42.50  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       25 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEItpDKAfqdKLYPFTWDAVRYNGKLI 104
Cdd:cd13662  17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKL--DKS---KLPNVKEEKDNLMEASK 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
3LC8_A      105 AY--------PIAVEALSLIYNKDLLPNPPKTWEeipALDRElKAKGKSALMFNLQE 153
Cdd:cd13662  92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKWS---IFLRE-DLAGRMTMLDDMRE 144
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 26-133 5.28e-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: 41.27  E-value: 5.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       26 KFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFwahdrFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRY----- 99
Cdd:cd13523  18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVT-----PSDSYTSRQLGVGLMQPIDKSLLPSWATLDPHLtlaav 92

                        90       100       110
                ....*....|....*....|....*....|....*..
3LC8_A      100 ---NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIP 133
Cdd:cd13523  93 ltvPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL 129
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 57-295 5.89e-04

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 41.19  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A         57 PDIIFWAHDRFGG------YAQSGLLAEITPDK-AFQDKLYPFTWdaVRYNGKLIaYPIAVEALSLIYNKDLLPN--PPK 127
Cdd:pfam13343   4 PDIILSAGDLFFDkrflekFIEEGLFQPLDSANlPNVPKDFDDEG--LRDPDGYY-TPYGVGPLVIAYNKERLGGrpVPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        128 TWEEIpaLDRELKakgKSALMFNLqePYFTWPLIAADGGYafkyengkydiKDVGVDnagakAGLTFLVDLIKNKHMNAD 207
Cdd:pfam13343  81 SWADL--LDPEYK---GKVALPGP--NVGDLFNALLLALY-----------KDFGED-----GVRKLARNLKANLHPAQM 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        208 TDYSiaeAAFNKGETAMTInGPWAWSNIDTSKVNYGVTVLPtfkgqPSKPFVGVLSAGINAAspNKELAKEFLeNYLLTD 287
Cdd:pfam13343 138 VKAA---GRLESGEPAVYL-MPYFFADILPRKKKNVEVVWP-----EDGALVSPIFMLVKKG--KKELADPLI-DFLLSP 205


                  ....*...
3LC8_A        288 EGLEAVNK 295
Cdd:pfam13343 206 EVQAILAK 213
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 25-165 1.89e-03

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 40.05  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        25 KKFEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPDKAfqDKLYPFTWD 95
Cdd:PRK15046  54 PAFTKATGIKVnyveagsgeVVNRAAK-EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKD 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A        96 AvryNGKLiaYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDRELKAKgksalmfnLQepYFTwPLIAADG 165
Cdd:PRK15046 124 A---DGTY--APFVNNYLSFIYNPKVLKTAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDG 175
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 21-131 2.77e-03

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 39.44  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       21 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPDKAFQDKLyPFTWDAv 97
Cdd:COG4143  48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                        90       100       110
                ....*....|....*....|....*....|....
3LC8_A       98 ryNGKLIayPIAVEALSLIYNKDLLPNPPKTWEE 131
Cdd:COG4143 126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLED 155
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 27-288 3.58e-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: 39.08  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       27 FEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAHdrfggyaQSGLLAEITPDKAFQDklypftwDAV 97
Cdd:cd13548  21 FTKATGITVnyveagsgeVVERAAK-EKSNPQADVLVTLPPFIQQAA-------QMGLLQPYQSDAAKNP-------AII 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A       98 RYNGKLIAyPIAVEALSLIYNKDLLPNPPKTWEEI--PALDREL------KAKGKSALMFNLQEpyftwpLIAADGGYAF 169
Cdd:cd13548  86 KAEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADLldPKYKGKIqystpgQAGDGMAVLLLTTH------LMGSDAAFAY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3LC8_A      170 kyengkydIKDVGVDNAGAKAGLTFLVDLIknkhmnadtdysiaeaafNKGETAMTiNG--PWAWSNIDTSKVNYGVtVL 247
Cdd:cd13548 159 --------LAKLQQNNVGPSASTGKLTALV------------------SKGEISVA-NGdlQMNLAQMEHANPNKKI-FW 210

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
3LC8_A      248 PTFKGQPSKPFVGVLSAGINAASPNKELAKEfLENYLLTDE 288
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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