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Conserved domains on  [gi|2447596932|pdb|8H68|A]
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Chain A, Maltose/maltodextrin-binding periplasmic protein,DNA N6-methyl adenine demethylase

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
2-369 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 807.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         2 SKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 81
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        82 TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 161
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       162 LIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK 241
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       242 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 321
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
8H68_A       322 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 369
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
2OG-FeII_Oxy super family cl21496
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 428-599 2.88e-04

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


The actual alignment was detected with superfamily member pfam13532:

Pssm-ID: 473886  Cd Length: 191  Bit Score: 42.30  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        428 GLTLIHNFLSESEESKILNMI-DTVEWAQS--QSGRR------------------KQDYGPKVNFKHKKvktdtFVGMPE 486
Cdd:pfam13532   1 GLVLLPGFLSPEEAAELLRELlEEGPFRQPttQGGRPmsvrmtncgqlgwvtdgpGYRYSGVDPVTGEP-----WPPFPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        487 YADMLLNKMSEYDvkKLGNYQPfEMC--NLeYEevKKSAIEMHQDDMWIW-GNRLISINLINGSVMTL---SNDNKSFLc 560
Cdd:pfam13532  76 ALLQLAERLAAEA--GYPGWSP-NAClvNF-YR--DGARMGLHQDRDESGpGAPIVSLSLGASATFRFggkSRSDPTIS- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
8H68_A        561 yVHMPHRSLLCMADECRYDWkHGVLahHIR--------GRRIALTMR 599
Cdd:pfam13532 149 -LRLESGDVLVMGGESRLAY-HGVP--PIRrgthpllgGGRINLTFR 191
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
2-369 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 807.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         2 SKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 81
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        82 TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 161
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       162 LIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK 241
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       242 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 321
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
8H68_A       322 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 369
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 7-369 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: 709.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        7 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 86
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       87 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 166
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      167 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 246
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      247 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 326
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
8H68_A      327 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 369
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-373 1.12e-150

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 441.31  E-value: 1.12e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        1 GSKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLL 78
Cdd:COG2182  33 SAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       79 AEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPY 157
Cdd:COG2182 112 APLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAY 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      158 FTWPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 237
Cdd:COG2182 192 YFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADL 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      238 DTS-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEEL 313
Cdd:COG2182 270 KKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEV 347

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      314 AKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAAL 373
Cdd:COG2182 348 KADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 24-317 1.03e-35

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 135.61  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         24 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 99
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        100 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 175
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        176 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 254
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
8H68_A        255 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 317
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
2OG-FeII_Oxy_2 pfam13532
2OG-Fe(II) oxygenase superfamily;
428-599 2.88e-04

2OG-Fe(II) oxygenase superfamily;


Pssm-ID: 433285  Cd Length: 191  Bit Score: 42.30  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        428 GLTLIHNFLSESEESKILNMI-DTVEWAQS--QSGRR------------------KQDYGPKVNFKHKKvktdtFVGMPE 486
Cdd:pfam13532   1 GLVLLPGFLSPEEAAELLRELlEEGPFRQPttQGGRPmsvrmtncgqlgwvtdgpGYRYSGVDPVTGEP-----WPPFPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        487 YADMLLNKMSEYDvkKLGNYQPfEMC--NLeYEevKKSAIEMHQDDMWIW-GNRLISINLINGSVMTL---SNDNKSFLc 560
Cdd:pfam13532  76 ALLQLAERLAAEA--GYPGWSP-NAClvNF-YR--DGARMGLHQDRDESGpGAPIVSLSLGASATFRFggkSRSDPTIS- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
8H68_A        561 yVHMPHRSLLCMADECRYDWkHGVLahHIR--------GRRIALTMR 599
Cdd:pfam13532 149 -LRLESGDVLVMGGESRLAY-HGVP--PIRrgthpllgGGRINLTFR 191
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
2-369 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 807.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         2 SKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 81
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        82 TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 161
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       162 LIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK 241
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       242 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 321
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
8H68_A       322 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 369
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKR 393
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 7-369 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: 709.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        7 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 86
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       87 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 166
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      167 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 246
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      247 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 326
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
8H68_A      327 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTN 369
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-373 1.12e-150

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 441.31  E-value: 1.12e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        1 GSKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLL 78
Cdd:COG2182  33 SAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       79 AEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPY 157
Cdd:COG2182 112 APLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAY 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      158 FTWPLIAADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 237
Cdd:COG2182 192 YFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADL 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      238 DTS-KVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEEL 313
Cdd:COG2182 270 KKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEV 347

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      314 AKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAAL 373
Cdd:COG2182 348 KADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 8-370 1.21e-149

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: 436.84  E-value: 1.21e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTVEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 83
Cdd:cd13522   1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       84 DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 162
Cdd:cd13522  81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      163 IAADGGYAFKYENGKYDIkdvGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID-TS 240
Cdd:cd13522 161 IGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRqAL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      241 KVNYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLeaVNKDKPLGAVALKSYEEELAKDPRI 319
Cdd:cd13522 238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
8H68_A      320 A--ATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNA 370
Cdd:cd13522 316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 8-370 3.65e-138

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: 407.45  E-value: 3.65e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 85
Cdd:cd13586   1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       86 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDK--ELKAKGKSALMFNLQEPYFTWPLI 163
Cdd:cd13586  81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQTNPYFSYPFL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      164 AADGGYAFKYENGkyDIKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 242
Cdd:cd13586 161 AAFGGYVFGENGG--DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      243 NYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPlGAVALKSYEE--ELAKDPRI 319
Cdd:cd13586 239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTG-RIPALKDALNdaAVKNDPLV 316

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
8H68_A      320 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNA 370
Cdd:cd13586 317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 8-366 1.32e-89

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


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 282.83  E-value: 1.32e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 85
Cdd:cd13658   1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       86 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 163
Cdd:cd13658  81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      164 AADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVN 243
Cdd:cd13658 161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      244 YGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PlGAVALKSYEEElAKDPRI 319
Cdd:cd13658 241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiP-PRKDVRSDPEI-KNNPLT 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
8H68_A      320 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 366
Cdd:cd13658 318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDA 364
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 8-367 8.62e-74

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: 241.13  E-value: 8.62e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT- 82
Cdd:cd13657   1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       83 ---PDKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPY 157
Cdd:cd13657  81 ylsEDDF--ENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      158 FTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI 237
Cdd:cd13657 159 FVSAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGI 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      238 DTSKVNYGVTVLPTFKGQ-PSKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDEGLEAVNKdkpLGAV--ALKSYEE- 311
Cdd:cd13657 233 KAAGIDLGVAPLPTVDGTnPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADE---NGYVpaATNAYDDa 309

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
8H68_A      312 ELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 367
Cdd:cd13657 310 EVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 8-370 5.35e-60

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: 205.33  E-value: 5.35e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKGY-NGLAEVGKKFEK-DTGIKVTVEhP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 82
Cdd:cd13585   1 TLTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVV-PvpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       83 P---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL------PNPPKTWEEIPALDKELKAKGKS----AL 149
Cdd:cd13585  80 DyieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLEAAKKLTDKKGGqygfAL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      150 MFNLQEPYFTWPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGETAMT 227
Cdd:cd13585 160 RGGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMM 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      228 INGPWAWSNIDTSKV--NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG---LEAVNKDKPLG 302
Cdd:cd13585 235 IDGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALA 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      303 AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASG--RQTVDEALKDAQTNA 370
Cdd:cd13585 314 AAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAKEI 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 8-370 2.92e-57

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: 197.90  E-value: 2.92e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWI-NGDKGYNGLAEVGKKFEK-DTGIKVTVEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 82
Cdd:cd14748   1 EITFWHgMSGPDGKALEELVDEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       83 P----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-------PNPPKTWEEI----PALDKELKAKGKS 147
Cdd:cd14748  81 DyidkDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFeeagldpEKPPKTWDELeeaaKKLKDKGGKTGRY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      148 ALMFNLQEPYFTW-PLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAM 226
Cdd:cd14748 161 GFALPPGDGGWTFqALLWQNGGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAM 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      227 TINGPWAWSNI--DTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDEGLEAVNKDK---P 300
Cdd:cd14748 236 TINGTWSLAGIrdKGAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylP 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
8H68_A      301 LGAVALKSYEEELAKDPRIAATMENAQKG-EIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNA 370
Cdd:cd14748 315 VRKSAAEDPEEFLAENPNYKVAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-373 5.91e-57

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 196.42  E-value: 5.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        5 EEGKLVIWINGDKGYNGLAEVGKKFEKDT-GIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 81
Cdd:COG1653  31 GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       82 TP----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAK-GKSALMFN 152
Cdd:COG1653 111 DDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEkaglDPPKTWDELLAAAKKLKAKdGVYGFALG 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      153 LQEPYFTWPLIAADGGYAFKyENGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAMTIN 229
Cdd:COG1653 191 GKDGAAWLDLLLSAGGDLYD-EDGK-----PAFDSPEAVEALEFLKDLVKDGYVPPGalgTDWDDARAAFASGKAAMMIN 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      230 GPWAWSNIDTS--KVNYGVTVLPTFK-GQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNkdkplgaval 306
Cdd:COG1653 265 GSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKWD---------- 333

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
8H68_A      307 ksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtAVINAASGRQTVDEALKDAQTNAAAL 373
Cdd:COG1653 334 -----------------------------------------ALQAVLLGQKTPEEALDAAQAAANAA 359
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 8-372 7.98e-43

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: 158.70  E-value: 7.98e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 81
Cdd:cd14749   1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       82 TP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-----NPPKTWEEIPALDKELKAKGK------S 147
Cdd:cd14749  81 TDyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKgqtgfgL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      148 ALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKdvgvDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGET 224
Cdd:cd14749 161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFN----DPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      225 AMTINGPWAWSNIDTSKV--NYGVTVLPTFK--GQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEA-VNKDK 299
Cdd:cd14749 236 AMNIGGSWDLGAIKAGEPggKIGVFPFPTVGkgAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQyLEDVG 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
8H68_A      300 PLGAVALKSYEEELAKDPRIAATME-NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAA 372
Cdd:cd14749 315 LLPAKEVVAKDEDPDPVAILGPFADvLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 17-367 4.14e-40

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


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 150.91  E-value: 4.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       17 KGYNGLAEVGKKFEKDT-GIKVTVE-HP---DKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITPD-- 84
Cdd:cd14750  11 QEGELLKKAIAAFEKKHpDIKVEIEeLPassDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEYlk 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       85 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAKGKSALMFNLQ----EP 156
Cdd:cd14750  87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      157 YFT--WPLIAADGGYAFKYENGKydikdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGETAMTINGP 231
Cdd:cd14750 167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      232 WAW--SNIDTSKVN--YGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALK 307
Cdd:cd14750 242 YAYalLQGPESAVAgkVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
8H68_A      308 SYEEE--LAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 367
Cdd:cd14750 321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQ 382
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 8-368 5.45e-40

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: 150.54  E-value: 5.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTVEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 79
Cdd:cd14747   1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       80 EITP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDKELKAKG--KSAL 149
Cdd:cd14747  77 DLTPyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLkkaggDEAPKTWDELEAAAKKIKADGpdVSGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      150 MF----NLQEPYFTWpLIAADGGYAfkyengKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGE 223
Cdd:cd14747 157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      224 TAMTINGPWAWSNIDTS----KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK 299
Cdd:cd14747 230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
8H68_A      300 PLGAvALKSY--EEELAKDPRIAATMENAQKGEIMPNIPQmsafWYAVRTAVINA-----ASGRQTVDEALKDAQT 368
Cdd:cd14747 309 GMLP-ANTSAwdDPSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVleevwIGVGADVEDALDKAAA 379
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 24-317 1.03e-35

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 135.61  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         24 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 99
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        100 RYNGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYEN 175
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        176 GKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLptfkg 254
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP----- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
8H68_A        255 qPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 317
Cdd:pfam13416 217 -KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 19-291 1.67e-35

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: 135.62  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         19 YNGLAEVGKKFEKD-TGIKVTVE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPf 94
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         95 twdavrynGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPLIAA 165
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        166 DGGYAFKYENGKYDiKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV- 242
Cdd:pfam01547 158 LGGPLFDKDGGGLD-NPEAVDAITYYVDLYAKVLLLKKLKNPgvAGADGREALALFEQGKAAMGIVGPWAALAANKVKLk 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
8H68_A        243 ------------NYGVTVLPTFKGQPskpfVGVLSAGINAASPNKELAKEFLeNYLLTDEG 291
Cdd:pfam01547 237 vafaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 29-368 9.97e-33

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: 129.81  E-value: 9.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       29 FEKDT-GIKVTVE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQD--KLYPFTWDAVRYNG 103
Cdd:cd14751  23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      104 KLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKYENGky 178
Cdd:cd14751 103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      179 DIKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV-----NYGVTVLPT 251
Cdd:cd14751 178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      252 FKGQPSKPfVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDPRIAATMENAQKGE 330
Cdd:cd14751 258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLGLLPTRTSAYEsPEVANNPMVAAFKPALETAV 335

                       330       340       350
                ....*....|....*....|....*....|....*...
8H68_A      331 IMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT 368
Cdd:cd14751 336 PRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAK 373
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 58-342 7.01e-26

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: 109.74  E-value: 7.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       58 GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-PNPPKTWEEI 134
Cdd:cd13655  53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLtEDDVKSLDTM 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      135 paLDKELKAKGKSAlmFNLQEPYFTWPLIAADGGYAFKyeNGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 214
Cdd:cd13655 133 --LAKAPDAKGKVS--FDLSNSWYLYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      215 AEAAFNKGETAMTINGPWAWSNI-----DtskvNYGVTVLPTFK--GQ--PSKPFVGVLSAGINAASPNKELAKEFLEnY 285
Cdd:cd13655 206 AISGLKDGTLGAGVSGPWDAANLkkalgD----NYAVAKLPTYTlgGKdvQMKSFAGYKAIGVNSNTKNPEAAMALAD-Y 280

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
8H68_A      286 LLTDEGLEAV---NKDKPLGAVALKSyeEELAKDPRIAATMENAQKGEI-MPNIPQMSAFW 342
Cdd:cd13655 281 LTNEESQLTRfekRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
5-346 2.17e-18

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 86.89  E-value: 2.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        5 EEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 84
Cdd:COG0687  27 AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVVPSDYFVARLIKAGLLQPLDKS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       85 K--AFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELkaKGKSALmfnLQEPYFTWPL 162
Cdd:COG0687 104 KlpNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL--WDPEY--KGKVAL---LDDPREVLGA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      163 IAADGGYAFkyengkYDIKDVGVDNAGAKagltflvdLIKNKHMNA--DTDYSIAEAAFNKGET--AMTINGPWAWSNID 238
Cdd:COG0687 176 ALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDGAEYIQLLASGEVdlAVGWSGDALALRAE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      239 TSKVNYgvtVLPTfKGQPSkpFVGVLSagINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLGAV---ALKSYEEELAK 315
Cdd:COG0687 242 GPPIAY---VIPK-EGALL--WFDNMA--IPKGAPNPDLAYAFI-NFMLSPEVAAALAEYVGYAPPnkaARELLPPELAA 312

                       330       340       350
                ....*....|....*....|....*....|....*.
8H68_A      316 DPRIAATMENAQKGEIMPNIP-----QMSAFWYAVR 346
Cdd:COG0687 313 NPAIYPPEEVLDKLEFWNPLPpenreLYTRRWTEIK 348
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 27-291 3.06e-14

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 73.43  E-value: 3.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       27 KKFEKDTGIKVTVEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPDKA------FQDKLYpfTWd 97
Cdd:COG1840   3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPELdaipaeFRDPDG--YW- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       98 avryngkliaYPIAVEALSLIYNKDLLP--NPPKTWEEIpaLDKELKAKgksalmfnlqepyFTWPLIAADG-GYAFkye 174
Cdd:COG1840  79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLL--- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      175 ngkydikdVG--VDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGETAMTINGPWAWSNIDTSKVNYGVtVLPTF 252
Cdd:COG1840 131 --------VAalLQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEV-VFPED 200

                       250       260       270
                ....*....|....*....|....*....|....*....
8H68_A      253 KGqpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEG 291
Cdd:COG1840 201 GT-----LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 24-287 8.47e-12

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


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 66.49  E-value: 8.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       24 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAVRY 101
Cdd:cd13590  14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      102 NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEiPALDKELkaKGKSAlMFNLQEPYFTWPLIAAdgGYAFkyengkYDIK 181
Cdd:cd13590  94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPAL--KGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      182 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGET--AMTINGPWAWSNIDTSKVNYgvtVLPTFKGQpskp 259
Cdd:cd13590 162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIPKEGGL---- 226

                       250       260
                ....*....|....*....|....*...
8H68_A      260 fVGVLSAGINAASPNKELAKEFLeNYLL 287
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 ...
 27-299 6.73e-11

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: 65.04  E-value: 6.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       27 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPdkaFQDKLYP--------FT 95
Cdd:cd13580  26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       96 WDAVRYNGKLIAYPIAVEALS---LIYNKDLLPN----PPKTWEEipaLDKELKAkgksalmFNLQEP-------YFTWP 161
Cdd:cd13580 103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKA-------FTEKDPdgngkkdTYGLT 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      162 LIAADGGYAFK--------YENGKYDIKDVGVDNAG----AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 226
Cdd:cd13580 173 DTKDLIGSGFTglfgafgaPPNNWWKDEDGKLVPGSiqpeMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGI 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      227 TINGPWAWSNIDTSKVNYG----VTVLPTFKGqPSKPFVGVLSAG------INAASPNKELAKEFL------ENYLLTDE 290
Cdd:cd13580 253 FVGNWWDPAWPQASLKKNDpdaeWVAVPIPSG-PDGKYGVWAESGvngffvIPKKSKKPEAILKLLdflsdpEVQKLLDY 331


                ....*....
8H68_A      291 GLEAVNKDK 299
Cdd:cd13580 332 GIEGVHYTV 340
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 23-302 9.86e-11

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: 62.63  E-value: 9.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       23 AEVGKKFEKDTGIKVTVEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAV 99
Cdd:cd13589  17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      100 RYngkliAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDKELKAK--GKSALmfNLQEPYFTWPLIAADGGyafkyengk 177
Cdd:cd13589  96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGKfpGPRIL--NTSGLALLEAALLADGV--------- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      178 yDIKDVGVDNAGAKagltflVDLIKNkhmNADTDY-SIAEAA--FNKGETAMTI--NGPWAWSNIDTSKVNYgvtVLPTf 252
Cdd:cd13589 157 -DPYPLDVDRAFAK------LKELKP---NVVTWWtSGAQLAqlLQSGEVDMAPawNGRAQALIDAGAPVAF---VWPK- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
8H68_A      253 kgqpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLG 302
Cdd:cd13589 223 ----EGAILGPDTLAIVKGAPNKELAMKFI-NFALSPEVQAALAEALGYG 267
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 8-296 4.82e-09

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: 57.70  E-value: 4.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        8 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTVEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 83
Cdd:cd13518   1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       84 DkafQDKLYPFTWDAVryNGKLiaYPIAVEALSLIYNKDLLPNP--PKTWEEIpaLDKELkaKGKSALMFNLQEPYFTWP 161
Cdd:cd13518  77 K---VIEAIPADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKW--KGKIVYPTPLRSGTGLTH 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      162 LIAAdggYAFKYE--NGKYDIKDVGvDNAGAKAGLTFLVDLIKNKHM---NADTDYSIAEAAfnKGETAMTINgpwawsn 236
Cdd:cd13518 146 VAAL---LQLMGEekGGWYLLKLLA-NNGKPVAGNSDAYDLVAKGEVavgLTDTYYAARAAA--KGEPVEIVY------- 212

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      237 idtskVNYGVTVLPTfkgqpskpfvgvlSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 296
Cdd:cd13518 213 -----PDQGALVIPE-------------GVALLKGAPNPEAAKKFID-FLLSPEGQKALA 253
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 23-127 4.32e-08

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


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 55.13  E-value: 4.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       23 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVR- 100
Cdd:cd13587  13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                        90       100       110
                ....*....|....*....|....*....|
8H68_A      101 ---YNGKLIAYPIAVEALSLIYNKDLLPNP 127
Cdd:cd13587  93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 25-291 9.92e-08

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: 54.77  E-value: 9.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       25 VGKKFEKDTGIK-VTVEHPDKL-EEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITPD-------KAFQDKLY 92
Cdd:cd13521  22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKYidqypnlKAFFKQHP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       93 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAK-----GKS-----ALMFNLQ 154
Cdd:cd13521 101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKdpngnGKAdeipfIDRDPLY 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      155 EPYFT---WPLIAADGG--YAFKYENGKydIKDVGVDNAgAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 226
Cdd:cd13521 181 GAFRLinsWGARSAGGStdSDWYEDNGK--FKHPFASEE-YKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKLGG 257

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
8H68_A      227 TINGPWAWSNIDT---SKVNYGVTVLPTFKGQPSKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDEG 291
Cdd:cd13521 258 FTHNWFASDNLFTaqlGKEKPMYILLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 17-144 1.51e-07

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 53.45  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       17 KGYnGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYP-F 94
Cdd:cd13588   8 PGY-ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrL 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
8H68_A       95 TW-DAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPAlDKELKAK 144
Cdd:cd13588  87 RNlPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW-DPKYKGR 136
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 24-295 2.68e-05

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


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 46.14  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       24 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPdkafqdKLYPFTWDAVR 100
Cdd:cd13545  19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      101 YNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEipaldkelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKYen 175
Cdd:cd13545  93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLL-- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      176 gkYDIKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGETAMTI---NGPwAWSNIDTSKVNYGVTVLPTf 252
Cdd:cd13545 152 --WTIAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
8H68_A      253 kGQpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAV 295
Cdd:cd13545 222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLSPEFQEVI 258
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 24-84 3.57e-05

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


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 46.20  E-value: 3.57e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
8H68_A       24 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 84
Cdd:cd13664  14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKS 74
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 28-144 5.15e-05

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


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 45.51  E-value: 5.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       28 KFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFwahdrFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRY----- 101
Cdd:cd13523  18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVT-----PSDSYTSRQLGVGLMQPIDKSLLPSWATLDPHLtlaav 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
8H68_A      102 ---NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPaLDKELKAK 144
Cdd:cd13523  93 ltvPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL-DDPKYKGR 137
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 59-297 9.80e-05

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 44.27  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A         59 PDIIFWAHDRFGG------YAQSGLLAEITPDK-AFQDKLYPFTWdaVRYNGKLIaYPIAVEALSLIYNKDLLPN--PPK 129
Cdd:pfam13343   4 PDIILSAGDLFFDkrflekFIEEGLFQPLDSANlPNVPKDFDDEG--LRDPDGYY-TPYGVGPLVIAYNKERLGGrpVPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        130 TWEEIpaLDKELKakgKSALMFNLqePYFTWPLIAADGGYafkyengkydiKDVGVDnagakAGLTFLVDLIKNKHMNAD 209
Cdd:pfam13343  81 SWADL--LDPEYK---GKVALPGP--NVGDLFNALLLALY-----------KDFGED-----GVRKLARNLKANLHPAQM 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        210 TDYSiaeAAFNKGETAMTInGPWAWSNIDTSKVNYGVTVLPtfkgqPSKPFVGVLSAGINAAspNKELAKEFLeNYLLTD 289
Cdd:pfam13343 138 VKAA---GRLESGEPAVYL-MPYFFADILPRKKKNVEVVWP-----EDGALVSPIFMLVKKG--KKELADPLI-DFLLSP 205


                  ....*...
8H68_A        290 EGLEAVNK 297
Cdd:pfam13343 206 EVQAILAK 213
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 27-298 1.77e-04

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 44.29  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        27 KKFEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPDKAfqDKLYPFTWD 97
Cdd:PRK15046  54 PAFTKATGIKVnyveagsgeVVNRAAK-EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        98 AvryNGKLiaYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELKAKgksalmfnLQepYFTwPLIAADGG-------YA 170
Cdd:PRK15046 124 A---DGTY--APFVNNYLSFIYNPKVLKTAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDGTavllltfHL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       171 FkyengkydikdvgvdnaGAKAGLTFLVDL-IKNKHMNADTDYsiAEAAFNKGETAMTiNG--PWAWSNIDTSKVNYGVT 247
Cdd:PRK15046 186 M-----------------GKDKAFDYLAKLqANNVGPSKSTGK--LTPLVSKGEIYVA-NGdlQMNLAQAEHGGPNVKIF 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
8H68_A       248 VLPTFKGQPSK---PFVgvlsAGINAASPNKELAKEFLEnYLLTDEGLEAVNKD 298
Cdd:PRK15046 246 FPAKDGGERSTfalPYV----IGLVKGAPNSENGKKLID-FLLSKEAQTKVSDM 294
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 29-290 1.95e-04

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


Pssm-ID: 270266 [Multi-domain]  Cd Length: 310  Bit Score: 43.70  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       29 FEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAHdrfggyaQSGLLAEITPDKAFQDklypftwDAV 99
Cdd:cd13548  21 FTKATGITVnyveagsgeVVERAAK-EKSNPQADVLVTLPPFIQQAA-------QMGLLQPYQSDAAKNP-------AII 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      100 RYNGKLIAyPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELKAK------GKS----ALMFNLQEpyftwpLIAADGGY 169
Cdd:cd13548  86 KAEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADL--LDPKYKGKiqystpGQAgdgmAVLLLTTH------LMGSDAAF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      170 AFkyengkydIKDVGVDNAGAKAGLTFLVDLIknkhmnadtdysiaeaafNKGETAMTiNG--PWAWSNIDTSKVNYGVt 247
Cdd:cd13548 157 AY--------LAKLQQNNVGPSASTGKLTALV------------------SKGEISVA-NGdlQMNLAQMEHANPNKKI- 208

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
8H68_A      248 VLPTF-KGQPSK---PFVgvlsAGINAASPNKELAKEfLENYLLTDE 290
Cdd:cd13548 209 FWPAKaGGQRSTfalPYG----IGLVKGAPNADNGKK-LIDFLLSKE 250
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 27-293 2.23e-04

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 44.27  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       27 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDII--FWaHDRFGGYAQSGLLAEITP--DKA--FQDKLYPFTW-- 96
Cdd:cd13583  24 KEIEEKTNVKFKRTPipSSDYETKRSLLIASGDAPDIIpvLY-PGEENEFVASGALLPISDylDYMpnYKKYVEKWGLgk 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       97 --DAVRY-NGKLIAYPIAVEA----LSLIYNKDL-----LPnPPKTWEEIPALDKELKAK-----------GKSALMFNL 153
Cdd:cd13583 103 elATGRQsDGKYYSLPGLHEDpgvqYSFLYRKDIfekagIK-IPTTWDEFYAALKKLKEKypdsypysdrwNSNALLLIA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      154 QEPYFTWpliaADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMN----ADTDySIAEAAFNKGETAMTIN 229
Cdd:cd13583 182 APAFGTT----AGWGFSNYTYDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDpesfTQTD-DQAKAKFLNGKSFVITT 256

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
8H68_A      230 GPW-----AWSNIDTSKVNYGVTVLPTFKGQ------PSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLE 293
Cdd:cd13583 257 NPQtvdelQRNLRAADGGNYEVVSITPPAGPagkainGSRLENGFMISSKAKDSKNFEALLQFL-DWLYSDEGQE 330
2OG-FeII_Oxy_2 pfam13532
2OG-Fe(II) oxygenase superfamily;
428-599 2.88e-04

2OG-Fe(II) oxygenase superfamily;


Pssm-ID: 433285  Cd Length: 191  Bit Score: 42.30  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        428 GLTLIHNFLSESEESKILNMI-DTVEWAQS--QSGRR------------------KQDYGPKVNFKHKKvktdtFVGMPE 486
Cdd:pfam13532   1 GLVLLPGFLSPEEAAELLRELlEEGPFRQPttQGGRPmsvrmtncgqlgwvtdgpGYRYSGVDPVTGEP-----WPPFPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A        487 YADMLLNKMSEYDvkKLGNYQPfEMC--NLeYEevKKSAIEMHQDDMWIW-GNRLISINLINGSVMTL---SNDNKSFLc 560
Cdd:pfam13532  76 ALLQLAERLAAEA--GYPGWSP-NAClvNF-YR--DGARMGLHQDRDESGpGAPIVSLSLGASATFRFggkSRSDPTIS- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
8H68_A        561 yVHMPHRSLLCMADECRYDWkHGVLahHIR--------GRRIALTMR 599
Cdd:pfam13532 149 -LRLESGDVLVMGGESRLAY-HGVP--PIRrgthpllgGGRINLTFR 191
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 23-142 8.50e-04

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 42.14  E-value: 8.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       23 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPDKAFQDKLyPFTWDAv 99
Cdd:COG4143  48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
8H68_A      100 ryNGKLIayPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELK 142
Cdd:COG4143 126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKDK 164
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 27-131 9.19e-04

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


Pssm-ID: 270380  Cd Length: 312  Bit Score: 41.73  E-value: 9.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       27 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEItpDKAfqdKLYPFTWDAVRYNGKLI 106
Cdd:cd13662  17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKL--DKS---KLPNVKEEKDNLMEASK 91

                        90       100       110
                ....*....|....*....|....*....|...
8H68_A      107 AY--------PIAVEALSLIYNKDLLPNPPKTW 131
Cdd:cd13662  92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKW 124
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 73-283 2.92e-03

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


Pssm-ID: 270269 [Multi-domain]  Cd Length: 267  Bit Score: 40.08  E-value: 2.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A       73 AQSGLLAEITPDkaFQDKLypftwDAVRYNGKLIAYPIAVEALSLIYNKDLL--PNPPKTWeeiPALDKElKAKGKSALm 150
Cdd:cd13551  66 KKQGLLVPYTPS--WAGEI-----PSALSDGDGYYYPLVQQPIVLAYNPDTMtdPDAPKSW---TDLAKP-KYKGKYEV- 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8H68_A      151 FNLQEPyfTWPLIAADGGYAFKYENGKYDIKDvgvdnagakAGLTFLVDLIKNKHMNADTDYSIaeAAFNKGETAMTIN- 229
Cdd:cd13551 134 PGLLGG--TGQAILAGILVRYLDPKGEYGVSD---------EGWQVLEDYFANGYPAQEGTDFY--APFADGQVPIGYLw 200

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
8H68_A      230 GPWAWSNIDTSKVNYGvtVLPTFKGQpskPFVgVLSAGINAASPNKELAKEFLE 283
Cdd:cd13551 201 SSGLAGIQKQYGVEFK--IVDPEIGV---PFV-TEQVGIVKGTKKEAEAKAFID 248
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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