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Conserved domains on  [gi|263256970|gb|EEZ28316|]
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ABC transporter, solute-binding protein [Bacteroides fragilis]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194651)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates such as amino acids, peptides, sugars, vitamins, and inorganic ions; similar to Streptococcus pneumoniae spermidine/putrescine ABC transporter substrate-binding protein; belongs to the type 2 periplasmic binding protein (PBP2) family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 31-398 5.92e-125

The 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 group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative 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, 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: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 365.46  E-value: 5.92e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQAYYkeqtgeDIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTv 110
Cdd:cd13663    1 TLKVYNWGEYIDPDLIDDFEKET------GIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDY- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fphspDYMNDVSPYIREQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRDAY 190
Cdd:cd13663   74 -----SKLPNVDKNINIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNILWNKKYKGKILMYDSPRDAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 191 GTAIIYAHARdlaggkvtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEAd 270
Cdd:cd13663  149 MVALKALGYS------------LNTTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEEN- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 271 avgVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPEIMEAKTDTTltyysdl 350
Cdd:cd13663  216 ---ENLDYVIPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEESI------- 285

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 263256970 351 syffgpgadslQIDKIQYPDRKVVERCAMIRDFGDKTKD-VLEIWSRIK 398
Cdd:cd13663  286 -----------KDDKIFYPDEDIYKKCEVFKYLGGDAKKeYNDLWLEVK 323
 
Name Accession Description Interval E-value
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 31-398 5.92e-125

The 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 group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative 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, 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: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 365.46  E-value: 5.92e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQAYYkeqtgeDIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTv 110
Cdd:cd13663    1 TLKVYNWGEYIDPDLIDDFEKET------GIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDY- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fphspDYMNDVSPYIREQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRDAY 190
Cdd:cd13663   74 -----SKLPNVDKNINIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNILWNKKYKGKILMYDSPRDAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 191 GTAIIYAHARdlaggkvtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEAd 270
Cdd:cd13663  149 MVALKALGYS------------LNTTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEEN- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 271 avgVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPEIMEAKTDTTltyysdl 350
Cdd:cd13663  216 ---ENLDYVIPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEESI------- 285

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 263256970 351 syffgpgadslQIDKIQYPDRKVVERCAMIRDFGDKTKD-VLEIWSRIK 398
Cdd:cd13663  286 -----------KDDKIFYPDEDIYKKCEVFKYLGGDAKKeYNDLWLEVK 323
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-398 1.74e-89

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 275.64  E-value: 1.74e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   1 MLMNKLLITLCLAASFMLSGCYNSGEpREKVLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEK 80
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAA-AEGTLNVYNWGGYIDPDVLEPFE----KETG--IKVVYDTYDSNEEMLAKLRA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  81 GHEDFDVVCPSEYIIERMLKKDLLLPIDtvfpHSP-DYMNDVSPYIReqiDKLSQPGRVashYAVCYMWGTAGILYNKAF 159
Cdd:COG0687   74 GGSGYDVVVPSDYFVARLIKAGLLQPLD----KSKlPNLANLDPRFK---DPPFDPGNV---YGVPYTWGTTGIAYNTDK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 160 VPDaDAESWSCLWDRKYAGKILMKDSYRDAYGTAIIYAhardlaGGKvtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWE 239
Cdd:COG0687  144 VKE-PPTSWADLWDPEYKGKVALLDDPREVLGAALLYL------GYD------PNSTDPADLDAAFELLIELKPNVRAFW 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 240 ADFG--KEMMTKNKAWLNMTWSGDAKWAIEEadavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIA 317
Cdd:COG0687  211 SDGAeyIQLLASGEVDLAVGWSGDALALRAE----GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVA 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 318 LRNMEASGYVSAV-ASPEIMEAKtdttltyysdlsyffgpgadsLQIDKIQYPDRKVVERCAMIRDFGDKT-KDVLEIWS 395
Cdd:COG0687  287 AALAEYVGYAPPNkAARELLPPE---------------------LAANPAIYPPEEVLDKLEFWNPLPPENrELYTRRWT 345


                 ...
gi 263256970 396 RIK 398
Cdd:COG0687  346 EIK 348
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
 12-326 2.34e-39

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 144.67  E-value: 2.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  12 LAASFMLSGCYNSGEPREKVLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIeKGHED--FDVVC 89
Cdd:PRK09501   9 LAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFT----KETG--IKVIYSTYESNETMYAKL-KTYKDgaYDLVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  90 PSEYIIERMLKKDLLLPIDTvfpHSPDYMNDVSPyireqiDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWS 169
Cdd:PRK09501  82 PSTYYVDKMRKEGMIQKIDK---SKLTNFSNLDP------DMLNKPFDPNNDYSIPYIWGATAIGVNSDAIDPKSVTSWA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 170 CLWDRKYAGKILMKDSYRDAYGTAIiyahaRDLA-GGKVTvedlmndySPRAMEIAEKYLKAMKPNIAGWEADFGKEMMT 248
Cdd:PRK09501 153 DLWKPEYKGSLLLTDDAREVFQMAL-----RKLGySGNTT--------DPKEIEAAYNELKKLMPNVAAFNSDNPANPYM 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 263256970 249 KNKAWLNMTWSGDAkWAIEEAdavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGY 326
Cdd:PRK09501 220 EGEVNLGMIWNGSA-FVARQA---GTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGY 293
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 53-335 5.79e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 109.42  E-value: 5.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   53 YKEQTGEDIRIVYQTF-DINEIMLTKIEKG-HEDFDVVCPSEYIIERMLKKDLLLPIDTVfphspDYMNDVSPYIREQID 130
Cdd:pfam13416   6 FEKKTGVTVEVEPQASnDLQAKLLAAAAAGnAPDLDVVWIAADQLATLAEAGLLADLSDV-----DNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  131 KlsqpgrvASHYAVCYMWGTAGIL-YNKAFVPDA--DAESWSCLWDR--KYAGKILMkdsYRDAYGTAIIYAHArdlAGG 205
Cdd:pfam13416  81 D-------GKLYGVPYAASTPTVLyYNKDLLKKAgeDPKTWDELLAAaaKLKGKTGL---TDPATGWLLWALLA---DGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  206 KVTVEDLMNDYSPRAMEiaekYLKAMKPNIAGWEA-DFGKEMMTKNKAWLNMTWSgdakWAIEEADAVGVDLDYVVPREG 284
Cdd:pfam13416 148 DLTDDGKGVEALDEALA----YLKKLKDNGKVYNTgADAVQLFANGEVAMTVNGT----WAAAAAKKAGKKLGAVVPKDG 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 263256970  285 SNIWYDGWVIPKYAGNPEAASY-FINFMCRPDIALRNMEASGYV----SAVASPEI 335
Cdd:pfam13416 220 SFLGGKGLVVPAGAKDPRLAALdFIKFLTSPENQAALAEDTGYIpankSAALSDEV 275
 
Name Accession Description Interval E-value
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 31-398 5.92e-125

The 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 group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative 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, 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: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 365.46  E-value: 5.92e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQAYYkeqtgeDIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTv 110
Cdd:cd13663    1 TLKVYNWGEYIDPDLIDDFEKET------GIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDY- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fphspDYMNDVSPYIREQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRDAY 190
Cdd:cd13663   74 -----SKLPNVDKNINIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNILWNKKYKGKILMYDSPRDAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 191 GTAIIYAHARdlaggkvtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEAd 270
Cdd:cd13663  149 MVALKALGYS------------LNTTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEEN- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 271 avgVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPEIMEAKTDTTltyysdl 350
Cdd:cd13663  216 ---ENLDYVIPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEESI------- 285

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 263256970 351 syffgpgadslQIDKIQYPDRKVVERCAMIRDFGDKTKD-VLEIWSRIK 398
Cdd:cd13663  286 -----------KDDKIFYPDEDIYKKCEVFKYLGGDAKKeYNDLWLEVK 323
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-398 1.74e-89

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 275.64  E-value: 1.74e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   1 MLMNKLLITLCLAASFMLSGCYNSGEpREKVLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEK 80
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAA-AEGTLNVYNWGGYIDPDVLEPFE----KETG--IKVVYDTYDSNEEMLAKLRA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  81 GHEDFDVVCPSEYIIERMLKKDLLLPIDtvfpHSP-DYMNDVSPYIReqiDKLSQPGRVashYAVCYMWGTAGILYNKAF 159
Cdd:COG0687   74 GGSGYDVVVPSDYFVARLIKAGLLQPLD----KSKlPNLANLDPRFK---DPPFDPGNV---YGVPYTWGTTGIAYNTDK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 160 VPDaDAESWSCLWDRKYAGKILMKDSYRDAYGTAIIYAhardlaGGKvtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWE 239
Cdd:COG0687  144 VKE-PPTSWADLWDPEYKGKVALLDDPREVLGAALLYL------GYD------PNSTDPADLDAAFELLIELKPNVRAFW 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 240 ADFG--KEMMTKNKAWLNMTWSGDAKWAIEEadavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIA 317
Cdd:COG0687  211 SDGAeyIQLLASGEVDLAVGWSGDALALRAE----GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVA 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 318 LRNMEASGYVSAV-ASPEIMEAKtdttltyysdlsyffgpgadsLQIDKIQYPDRKVVERCAMIRDFGDKT-KDVLEIWS 395
Cdd:COG0687  287 AALAEYVGYAPPNkAARELLPPE---------------------LAANPAIYPPEEVLDKLEFWNPLPPENrELYTRRWT 345


                 ...
gi 263256970 396 RIK 398
Cdd:COG0687  346 EIK 348
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 31-332 6.39e-76

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: 239.83  E-value: 6.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEKG-HEDFDVVCPSEYIIERMLKKDLLLPIDt 109
Cdd:cd13590    1 ELNIYNWSDYIDPEVLKAFE----KETG--VKVNYDTYDSNEEMLAKLRAGgGSGYDLVVPSDYMVERLIKQGLLEPLD- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 110 vfpHS--PDYMNDVSPYIREQIDklsqPGRvasHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYR 187
Cdd:cd13590   74 ---HSklPNLKNLDPQFLNPPYD----PGN---RYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLWDPALKGRIAMLDDAR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 188 DAYGTAIIYAhardlagGKVtvedlMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIE 267
Cdd:cd13590  144 EVLGAALLAL-------GYS-----PNTTDPAELAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANR 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 263256970 268 EADavgvDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVAS 332
Cdd:cd13590  212 ENP----NLKFVIPKEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKA 272
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
 31-334 5.72e-60

The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative 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: 270377 [Multi-domain]  Cd Length: 331  Bit Score: 198.71  E-value: 5.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDtv 110
Cdd:cd13659    1 TLNVYNWSDYIAPDTLEDFE----KETG--IKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLD-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fpHS--PDYMNdvspyIREQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFV----PDADAESWSCLWDRKYAGK----- 179
Cdd:cd13659   73 --KSklPNWKN-----LDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVkaalGDDLPDSWDLVFDPENLSKlkscg 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 180 ILMKDSYRDAYGTAIIYaHARDLaggkvtvedlmNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWS 259
Cdd:cd13659  146 VSVLDSPEEVFPAALNY-LGLDP-----------NSTDPEDIKAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWS 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 263256970 260 GDAKWAIEEADAVG--VDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPE 334
Cdd:cd13659  214 GDAVQAAQRAKEAGngVTLEYVIPKEGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAAT 290
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 31-317 1.15e-43

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: 154.13  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKI-EKGHEDFDVVCPSEYIIERMLKKDLLLPIDT 109
Cdd:cd13523    1 TVVIYTWGGYLPQDIIDPFE----KETG--IKVVVDTAANSERMIKKLsAGGSGGFDLVTPSDSYTSRQLGVGLMQPIDK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 110 VFPHSPDYMNDVSpyireqiDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRDA 189
Cdd:cd13523   75 SLLPSWATLDPHL-------TLAAVLTVPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADLDDPKYKGRVSFSDIPRET 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 190 YGTAIIYAhardlagGKVTVEDLMNDYSPRameiAEKYLKAMKPNIAGW--EADFGKEMMTKNKAWLNMTWSGDA-KWAI 266
Cdd:cd13523  148 FAMALANL-------GADGNEELYPDFTDA----AAALLKELKPNVKKYwsNASQPANLLLNGEVVLAMAWLGSGfKLKQ 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 263256970 267 EeadavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIA 317
Cdd:cd13523  217 A-----GAPIEFVVPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVA 262
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
 31-328 3.73e-42

The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative 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: 270378 [Multi-domain]  Cd Length: 315  Bit Score: 151.58  E-value: 3.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEK-GHEDFDVVCPSEYIIERMLKKDLLLPIDT 109
Cdd:cd13660    1 TLNFYNWSEYVPPELLEQFT----KETG--IKVILSTYESNETMYAKVKLyKDGAYDLVVPSTYYVDKMRKEGLIQKIDK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 110 vfPHSPDYMNdVSPyireqiDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRDA 189
Cdd:cd13660   75 --SKITNFSN-IDP------DFLNQPFDPNNDYSIPYIWGATALAVNGDAVDGKSVTSWADLWKPEYKGKLLLTDDAREV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 190 YGTAIiyahardlaggkVTVEDLMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEa 269
Cdd:cd13660  146 FQMAL------------RKLGYSGNTKDPEEIEAAFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQA- 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 263256970 270 davGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVS 328
Cdd:cd13660  213 ---NKPIHVVWPKEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPT 268
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 32-334 1.00e-39

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: 144.81  E-value: 1.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  32 LKIYNWADYIGDGVLEDFQAyykeQTGedIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDtvf 111
Cdd:cd13664    2 LNLYNWTDYTSPELLDKFEK----ETG--IKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLD--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 112 PHSPDYMNDVSPYIReqiDKLSQPGRVashYAVCYMWGTAGILYNKAFVPDaDAESWSCLWD--RKYAGKILMKDSYRDA 189
Cdd:cd13664   73 KSQLTNYDNIDPRWR---KPDFDPGNE---YSIPWQWGTTGFAVDTAVYDG-DIDDYSVIFQppEELKGKIAMVDSMNEV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 190 YGTAIIYAhardlaGGKVTVEDlmndysPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEA 269
Cdd:cd13664  146 VNAAIYYL------GGPICTTD------PKLMRKVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRARRQN 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 263256970 270 DavgvDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPE 334
Cdd:cd13664  214 P----SLAYAYPKEGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAE 274
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
 12-326 2.34e-39

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 144.67  E-value: 2.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  12 LAASFMLSGCYNSGEPREKVLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIeKGHED--FDVVC 89
Cdd:PRK09501   9 LAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFT----KETG--IKVIYSTYESNETMYAKL-KTYKDgaYDLVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  90 PSEYIIERMLKKDLLLPIDTvfpHSPDYMNDVSPyireqiDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWS 169
Cdd:PRK09501  82 PSTYYVDKMRKEGMIQKIDK---SKLTNFSNLDP------DMLNKPFDPNNDYSIPYIWGATAIGVNSDAIDPKSVTSWA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 170 CLWDRKYAGKILMKDSYRDAYGTAIiyahaRDLA-GGKVTvedlmndySPRAMEIAEKYLKAMKPNIAGWEADFGKEMMT 248
Cdd:PRK09501 153 DLWKPEYKGSLLLTDDAREVFQMAL-----RKLGySGNTT--------DPKEIEAAYNELKKLMPNVAAFNSDNPANPYM 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 263256970 249 KNKAWLNMTWSGDAkWAIEEAdavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGY 326
Cdd:PRK09501 220 EGEVNLGMIWNGSA-FVARQA---GTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGY 293
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 31-331 5.60e-39

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: 142.19  E-value: 5.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQAyykeQTGedIRIVYQTFDINEIMLTKIEK-GHEDFDVVCPSEYIIERMLKKDLLLPIDT 109
Cdd:cd13587    1 TLRILTWAGYAPEDLLEKFEN----ETG--IKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 110 vfphSPDYMNDVSPYIREQIDKLSQ-PGRVashYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKIlmkdSYR- 187
Cdd:cd13587   75 ----SKIKVAQFPPSLLESTKLGTTiNGKR---YAVPFDWGTEGLTVNSTKAPDVSGFSYGDLWAPEYAGKV----AYRl 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 188 -DAYGTAIIYAHARdlagGKVTVeDLMNDY-SPRAM----EIAEKYLKAMKPNI-AGWE-ADFGKEMMTKNKAWLNMTWS 259
Cdd:cd13587  144 kSPLTGLGLYADAT----GEDPF-NRYLDYkDEAKYqkilDQVLQFLIERKANVkAYWNnADEALAAFRSGGCVIGQTWD 218

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 263256970 260 GDAkWAIEeadAVGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVA 331
Cdd:cd13587  219 STG-LKLN---RENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAV 286
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 31-331 4.09e-38

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: 139.74  E-value: 4.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDgvleDFQAYYKEQTGedIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTv 110
Cdd:cd13588    1 ELNVLTWPGYADP----DWVTAFEEATG--CKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDT- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fphS--PDYmNDVSPYIReQIDKLSQPGRVashYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKDSYRD 188
Cdd:cd13588   74 ---SkiPNY-ANIDPRLR-NLPWLTVDGKV---YGVPYDWGANGLAYNTKKVKTPPTSWLALLWDPKYKGRVAARDDPID 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 189 AYGTAIIYAHARDlaGGKVTVEDlmndyspraMEIAEKYLKAMKPNIAGWEADFGKEM--MTKNKAWLNMTWSGDAKwAI 266
Cdd:cd13588  146 AIADAALYLGQDP--PFNLTDEQ---------LDAVKAKLREQRPLVRKYWSDGAELVqlFANGEVVAATAWSGQVN-AL 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 263256970 267 EEAdavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVA 331
Cdd:cd13588  214 QKA---GKPVAYVIPKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNP 275
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 31-317 5.23e-34

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: 129.56  E-value: 5.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDGVLEDFQAYYkeqtgeDIRIVYQTFDINEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTv 110
Cdd:cd13662    1 VLYIYNWTYYIPDKVIEDFEKET------GIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDK- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 111 fPHSPDYMNDVSPYIReqIDKLSQPGrvaSHYAVCYMWGTAGILYNKAFVPDaDAESWSCLWDRKYAGKILMKDSYRDAY 190
Cdd:cd13662   74 -SKLPNVKEEKDNLME--ASKIYDPG---LEYSVPYMFGATGIAVNKKIVKN-YFRKWSIFLREDLAGRMTMLDDMREVI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 191 GTAIIYAhardlaGGKVtvedlmNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAIEEAD 270
Cdd:cd13662  147 GAALAYL------GYPV------DSKDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEE 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 263256970 271 AVGVDLdYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIA 317
Cdd:cd13662  215 EEKFDF-FIPEGAASMMYIDSFVIPKGSKHKDNAYKFINFILRPENY 260
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
 12-316 6.66e-33

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 127.66  E-value: 6.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  12 LAASFMLSGCYNSGEPREKVLKIYNWADYIGDGVLEDFQayykEQTGedIRIVYQTFDINEIMLTKIEKGHEDFDVVCPS 91
Cdd:PRK10682  12 LVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFE----KETG--IKVVYDVFDSNEVLEGKLMAGSTGFDLVVPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  92 EYIIERMLKKDLLLPIDTvfPHSPDYMNdVSPYIREQIDKlSQPGrvaSHYAVCYMWGTAGILYN-----KAFVPDADAE 166
Cdd:PRK10682  86 ASFLERQLTAGVFQPLDK--SKLPNWKN-LDPELLKLVAK-HDPD---NKYAMPYMWATTGIGYNvdkvkAVLGEDAPVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 167 SWSCLWDRKYAGKilMKD---SYRDA----YGTAIIYAhardlagGKVTVEDLMNDYSPRAMEIaekyLKAMKPNIAGWE 239
Cdd:PRK10682 159 SWDLVLKPENLEK--LKScgvSFLDApeeiFATVLNYL-------GKDPNSTKADDYTGPATDL----LLKLRPNIRYFH 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 263256970 240 ADFGKEMMTKNKAWLNMTWSGDAKWAIEEADAV--GVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDI 316
Cdd:PRK10682 226 SSQYINDLANGDICVAIGWAGDVWQASNRAKEAknGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDV 304
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 32-326 6.78e-30

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: 116.94  E-value: 6.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  32 LKIYNWADYIGDGVLEDFQAYYKEQTGedIRIVYQTFDiNEIMLTKI--EKGHEDFDVVCPSEYIIERMLKKDLLLPIDT 109
Cdd:cd13589    2 LVVATWGGSYEDAQRKAVIEPFEKETG--IKVVYDTGT-SADRLAKLqaQAGNPQWDVVDLDDGDAARAIAEGLLEPLDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 110 -VFPhspdymNDVSPYIREqidklsqpgRVASHYAVCYMWGTAGILYNKAFVPDADAeSWScLWDRKYAGKILMKDSYRD 188
Cdd:cd13589   79 sKIP------NAAKDKAPA---------ALKTGYGVGYTLYSTGIAYNTDKFKEPPT-SWW-LADFWDVGKFPGPRILNT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 189 aYGTAIIYAhARDLAGGKVTVEDlmndyspraMEIAEKYLKAMKPNIAGWEADFGK--EMMTKNKAWLNMTWSGDAKWAI 266
Cdd:cd13589  142 -SGLALLEA-ALLADGVDPYPLD---------VDRAFAKLKELKPNVVTWWTSGAQlaQLLQSGEVDMAPAWNGRAQALI 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 267 EEadavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGY 326
Cdd:cd13589  211 DA----GAPVAFVWPKEGAILGPDTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGY 266
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 53-335 5.79e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 109.42  E-value: 5.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   53 YKEQTGEDIRIVYQTF-DINEIMLTKIEKG-HEDFDVVCPSEYIIERMLKKDLLLPIDTVfphspDYMNDVSPYIREQID 130
Cdd:pfam13416   6 FEKKTGVTVEVEPQASnDLQAKLLAAAAAGnAPDLDVVWIAADQLATLAEAGLLADLSDV-----DNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  131 KlsqpgrvASHYAVCYMWGTAGIL-YNKAFVPDA--DAESWSCLWDR--KYAGKILMkdsYRDAYGTAIIYAHArdlAGG 205
Cdd:pfam13416  81 D-------GKLYGVPYAASTPTVLyYNKDLLKKAgeDPKTWDELLAAaaKLKGKTGL---TDPATGWLLWALLA---DGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  206 KVTVEDLMNDYSPRAMEiaekYLKAMKPNIAGWEA-DFGKEMMTKNKAWLNMTWSgdakWAIEEADAVGVDLDYVVPREG 284
Cdd:pfam13416 148 DLTDDGKGVEALDEALA----YLKKLKDNGKVYNTgADAVQLFANGEVAMTVNGT----WAAAAAKKAGKKLGAVVPKDG 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 263256970  285 SNIWYDGWVIPKYAGNPEAASY-FINFMCRPDIALRNMEASGYV----SAVASPEI 335
Cdd:pfam13416 220 SFLGGKGLVVPAGAKDPRLAALdFIKFLTSPENQAALAEDTGYIpankSAALSDEV 275
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 3-334 1.11e-19

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 90.10  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   3 MNKLLITLCLAASFMLSGCYNSGEPR-----EKVLKIYNWADYIGDGVLEDFQAYYKEQTGEDIRIVYQTF-DINEIMLT 76
Cdd:COG1653    1 MRRLALALAAALALALAACGGGGSGAaaaagKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYdDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  77 KIEKGhEDFDVVCPSEYIIERMLKKDLLLPIDTVFPHSPDYMNDVSPYIRE--QIDklsqpGRVashYAVCYMWGTAGIL 154
Cdd:COG1653   81 ALAAG-NAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDagTYD-----GKL---YGVPFNTDTLGLY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 155 YNKAFVPDADAES-WSclWD--RKYAGKI--------LMKDSYRDAYGTAIIYAHARDL--AGGKVTVEdlmndySPRAM 221
Cdd:COG1653  152 YNKDLFEKAGLDPpKT--WDelLAAAKKLkakdgvygFALGGKDGAAWLDLLLSAGGDLydEDGKPAFD------SPEAV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 222 EIAEKYLKAMK-----PNIAGWEADFGKEMMTKNKAWlnMTWSGDakWAIEEADAVGVDLDYVV---------PREGSNI 287
Cdd:COG1653  224 EALEFLKDLVKdgyvpPGALGTDWDDARAAFASGKAA--MMINGS--WALGALKDAAPDFDVGVaplpggpggKKPASVL 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 263256970 288 WYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVASPE 334
Cdd:COG1653  300 GGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKWDALQAVLLGQKTPE 346
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 45-311 2.85e-14

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 73.05  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  45 VLEDFQayykEQTGEDIRIVYqtfDINEIMLTKI--EKGHEDFDVV-CPSEYIIERMLKKDLLLPIDtvfphsPDYMNDV 121
Cdd:COG1840    1 LLEAFE----KKTGIKVNVVR---GGSGELLARLkaEGGNPPADVVwSGDADALEQLANEGLLQPYK------SPELDAI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 122 SPYIREqidklsqpgrvASHYAVCYMWGTAGILYNKAFVPDADA-ESWSCLWDRKYAGKILMKDSYRDAYGTAIIYAhAR 200
Cdd:COG1840   68 PAEFRD-----------PDGYWFGFSVRARVIVYNTDLLKELGVpKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAA-LL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 201 DLAGGkvtvedlmndyspramEIAEKYLKAMKPNIAGWEADFGK--EMMTKNKAWLNMTWSGDAKWAIEEadavGVDLDY 278
Cdd:COG1840  136 QAFGE----------------EKGWEWLKGLAANGARVTGSSSAvaKAVASGEVAIGIVNSYYALRAKAK----GAPVEV 195

                        250       260       270
                 ....*....|....*....|....*....|...
gi 263256970 279 VVPREGSNIWYDGWVIPKYAGNPEAASYFINFM 311
Cdd:COG1840  196 VFPEDGTLVNPSGAAILKGAPNPEAAKLFIDFL 228
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 91-330 4.33e-13

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 68.93  E-value: 4.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   91 SEYIIERMLKKDLLLPIDTVfphSPDYMNDVSPYIreqidKLSQPGrvaSHYAVcYMWGTAGILYNKAFVPDADA-ESWS 169
Cdd:pfam13343  16 DKRFLEKFIEEGLFQPLDSA---NLPNVPKDFDDE-----GLRDPD---GYYTP-YGVGPLVIAYNKERLGGRPVpRSWA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  170 CLWDRKYAGKILMKDSYRDAYGTAIIYAHARD--LAGGKVTVEDLMNDYSPRAMeiaekyLKAMKPNIAGweadfgkemm 247
Cdd:pfam13343  84 DLLDPEYKGKVALPGPNVGDLFNALLLALYKDfgEDGVRKLARNLKANLHPAQM------VKAAGRLESG---------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  248 tKNKAWLNMTWSGDAkwaieeADAVGVDLDYVVPREGSNIWYDGWVIPKyaGNPEAASYFINFMCRPDIAlRNMEASGYV 327
Cdd:pfam13343 148 -EPAVYLMPYFFADI------LPRKKKNVEVVWPEDGALVSPIFMLVKK--GKKELADPLIDFLLSPEVQ-AILAKAGLV 217


                  ...
gi 263256970  328 SAV 330
Cdd:pfam13343 218 FPV 220
PBP2_PotD_PotF_like_1 cd13661
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 142-396 6.29e-11

The 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 group represents the periplasmic binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from plants and plant-symbiotic cyanobacteria. 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: 270379 [Multi-domain]  Cd Length: 319  Bit Score: 63.21  E-value: 6.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 142 YAVCYMWGTAGILYNKAFVPDA--DAESWSCLWDRKYAGKILMKDSYRDAYGtAIIYAHARDLAGGKVTVEDlmNDYSPR 219
Cdd:cd13661   81 WAVPYRWGTTVIAYRKDKLKKLgwDPIDWSDLWRPELAGRIAMVDSPREVIG-LVLKKLGASYNTAEVPGGR--EALEER 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 220 AMEIAEK--------YLKAMkpnIAGweadfgkemmtknKAWLNMTWSGDAKWAIEEADAVGVdldyVVPREGSNIWYDG 291
Cdd:cd13661  158 LAALRRQvklyssnnYLQAL---LLG-------------DVWVAVGWSQDIIPLARRYSNLAV----VIPRSGTSLWADL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 292 WVIPK-------YAGNPEAASYFINFMCRPDIALRnmeASGYVSAVASPEIMEAKTDT-TLTYYSDLSYFFGPGadslqi 363
Cdd:cd13661  218 WVIPAgsdfggrVRGPSPLLSQWIDFCLQPARATQ---FAQLSFGGASPLILDGPSLTpPEATRKLKLDTNLVL------ 288

                        250       260       270
                 ....*....|....*....|....*....|....
gi 263256970 364 dkiQYPDRKVVERCAMIRDFGDKT-KDVLEIWSR 396
Cdd:cd13661  289 ---GLPPDEILAKSEFLLPLSEATlAQYRALWQT 319
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 47-311 2.54e-09

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: 58.20  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   47 EDFQAYYKEQTGEDIRIVYQTFD-INEIMLTKIEKGHEDFDVVCPSEYIIERMLKKDLLLPIDTvfphspdymnDVSPYI 125
Cdd:pfam01547  12 ALVKEFEKEHPGIKVEVESVGSGsLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDD----------YVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  126 REQIDKLsqpgrvashYAVCYMWGTAGILYNKAFVPDADAESWScLWDRKYAGKILMKDSYRDAYG---------TAIIY 196
Cdd:pfam01547  82 VLGVPKL---------YGVPLAAETLGLIYNKDLFKKAGLDPPK-TWDELLEAAKKLKEKGKSPGGagggdasgtLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  197 AHARDLAGGKVTVEDLMNDYSPRAMEIAEKYLKAMK----------PNIAGWEADFGKEMMTKNKAWLNMTWSGDAKWAI 266
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAkvlllkklknPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 263256970  267 EEADAVGVDLDY-----------VVPREGSNIWYDGWVIPKYAGNPEAASYFINFM 311
Cdd:pfam01547 232 KVKLKVAFAAPApdpkgdvgyapLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFL 287
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-332 6.03e-09

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 57.65  E-value: 6.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   3 MNK---LLITLCLAASFMLSGC--------YNSGEPREKVLKIynWADYIGDGVLEDFQAYYKEQTGEDIRIVYQTF-DI 70
Cdd:COG2182    1 MKRrllAALALALALALALAACgsgssssgSSSAAGAGGTLTV--WVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWdDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  71 NEIMLTKIeKGHEDFDVVC-PSEYIiERMLKKDLLLPIDtvfphspDYMNDVSPYIREQIDKLSQPGRVashYAVCYMWG 149
Cdd:COG2182   79 REKLTTAA-PAGKGPDVFVgAHDWL-GELAEAGLLAPLD-------DDLADKDDFLPAALDAVTYDGKL---YGVPYAVE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 150 TAGILYNKAFVPDADAESWSCLWDrkyAGKILMKD-------SYRDAYGT-AIIYAhardlAGGKVTVEDLMNDY----- 216
Cdd:COG2182  147 TLALYYNKDLVKAEPPKTWDELIA---AAKKLTAAgkyglayDAGDAYYFyPFLAA-----FGGYLFGKDGDDPKdvgln 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 217 SPRAMEIAEKYLK-----AMKPNIAGweaDFGKEMMTKNKAwlNMTWSGDakWAIEEA-DAVGVDLDyVVP----REGSN 286
Cdd:COG2182  219 SPGAVAALEYLKDlikdgVLPADADY---DAADALFAEGKA--AMIINGP--WAAADLkKALGIDYG-VAPlptlAGGKP 290

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 263256970 287 ----IWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSAVAS 332
Cdd:COG2182  291 akpfVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKA 340
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 32-334 5.48e-08

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: 54.72  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  32 LKIYNWADYIGDGVLEDFQAYYkEQTGEDIRIVYQTFDiNEIMLTKIE---KGHEDFDVV-CPSEYIIErMLKKDLLLPI 107
Cdd:cd13585    2 LTFWDWGQPAETAALKKLIDAF-EKENPGVKVEVVPVP-YDDYWTKLTtaaAAGTAPDVFyVDGPWVPE-FASNGALLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 108 DtvfphspDYMNDvspyirEQIDKLSQPGRVAS------HYAVCYMWGTAGILYNK-----AFVPDADAESWSclWDRKY 176
Cdd:cd13585   79 D-------DYIEK------DGLDDDFPPGLLDAgtydgkLYGLPFDADTLVLFYNKdlfdkAGPGPKPPWTWD--ELLEA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 177 AGKIlmKDSYRDAYGTAI-------------IYAhardlAGGKVTVED----LMNdySPRAMEIAEKYLKAMK----PNI 235
Cdd:cd13585  144 AKKL--TDKKGGQYGFALrggsggqtqwypfLWS-----NGGDLLDEDdgkaTLN--SPEAVEALQFYVDLYKdgvaPSS 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 236 AGWEADFGKEMMTKNKAwlNMTWSGDakWAIEEADAVGVDLDYVV--------PREGSNIWYDGWVIPKYAGNPEAASYF 307
Cdd:cd13585  215 ATTGGDEAVDLFASGKV--AMMIDGP--WALGTLKDSKVKFKWGVaplpagpgGKRASVLGGWGLAISKNSKHPEAAWKF 290

                        330       340
                 ....*....|....*....|....*..
gi 263256970 308 INFMCRPDIALRNMEASGYVSAVASPE 334
Cdd:cd13585  291 IKFLTSKENQLKLGGAAGPAALAAAAA 317
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 43-366 6.58e-08

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: 54.22  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  43 DGVLEDFQAyykeqTGEDIRIVYQTFDINEIMLTKIE---KGHEDFDVVCPSEYIIERMLKKDLLLPIDTVFPHSPDYMN 119
Cdd:cd14748   17 EELVDEFNK-----SHPDIKVKAVYQGSYDDTLTKLLaalAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDKDGVDDD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 120 DVSPYIRE--QIDklsqpGRVashYAVCYMWGTAGILYNKA------FVPDADAESWSCLwdRKYAGKILMKDSYRDAYG 191
Cdd:cd14748   92 DFYPAALDagTYD-----GKL---YGLPFDTSTPVLYYNKDlfeeagLDPEKPPKTWDEL--EEAAKKLKDKGGKTGRYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 192 TAIIYAHARDL-------AGGKVTVED----LMNdySPRAMEIAEKYLK-AMKPNIAGWE-ADFGKEMMTKNKAwlNMTW 258
Cdd:cd14748  162 FALPPGDGGWTfqallwqNGGDLLDEDggkvTFN--SPEGVEALEFLVDlVGKDGVSPLNdWGDAQDAFISGKV--AMTI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 259 SGDakWAIEEADAVGVDLDY-VVP-------REGSNIWYDGWVIPK-YAGNPEAASYFINFMCRPDIALRNMEASGYV-- 327
Cdd:cd14748  238 NGT--WSLAGIRDKGAGFEYgVAPlpagkgkKGATPAGGASLVIPKgSSKKKEAAWEFIKFLTSPENQAKWAKATGYLpv 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 263256970 328 --SAVASPEIMEAKTDTTLTYYSDLSYFF---GPGADSLQIDKI 366
Cdd:cd14748  316 rkSAAEDPEEFLAENPNYKVAVDQLDYAKpwgPPVPNGAEIRDE 359
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 123-315 4.19e-06

Substrate binding domain of a putative iron transporter BitB, 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: 270264 [Multi-domain]  Cd Length: 258  Bit Score: 48.02  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 123 PYIREQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADA-ESWSCLWDRKYAGKILMKDSYRDAYGTAIIYAHARD 201
Cdd:cd13546   71 PYESPEAAAIPDAYKSPEGLWTGFSVLPVVLMVNTDLVKNIGApKGWKDLLDPKWKGKIAFADPNKSGSAYTILYTILKL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 202 LAGGKVTVEDLMNDysprAMEIAEKYlKAMKPNIAgweadfgkemmtKNKAWLNMTWSGDAKWAIEEADavgvDLDYVVP 281
Cdd:cd13546  151 YGGAWEYIEKLLDN----LGVILSSS-SAVYKAVA------------DGEYAVGLTYEDAAYKYVAGGA----PVKIVYP 209

                        170       180       190
                 ....*....|....*....|....*....|....
gi 263256970 282 REGSNIWYDGWVIPKYAGNPEAASYFINFMCRPD 315
Cdd:cd13546  210 KEGTTAVPDGVAIVKGAKNPENAKKFIDFLLSKE 243
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 31-316 5.12e-06

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: 47.68  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  31 VLKIYNWADYIGDG-VLEDFqayyKEQTGEDIRIVYqtfDINEIMLTKI--EKGHEDFDVVCPSEYI-IERMLKKDLLLP 106
Cdd:cd13518    1 ELVVYTASDRDFAEpVLKAF----EEKTGIKVKAVY---DGTGELANRLiaEKNNPQADVFWGGEIIaLEALKEEGLLEP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 107 IDTvfphspdymndvspyirEQIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAE-SWSCLWDRKYAGKILMKDS 185
Cdd:cd13518   74 YTP-----------------KVIEAIPADYRDPDGYWVGFAARARVFIYNTDKLKEPDLPkSWDDLLDPKWKGKIVYPTP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 186 YRDAYGT----AIIYAHARDLAGgkvtvedlmndysPRAMEIAEKYLKAMKPN------IAGWEADFGkemmtknkawln 255
Cdd:cd13518  137 LRSGTGLthvaALLQLMGEEKGG-------------WYLLKLLANNGKPVAGNsdaydlVAKGEVAVG------------ 191

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 263256970 256 MTWSGDakWAIEEADavGVDLDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDI 316
Cdd:cd13518  192 LTDTYY--AARAAAK--GEPVEIVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 53-348 2.84e-05

Substrate binding domain of a putative ferric iron 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: 270262 [Multi-domain]  Cd Length: 292  Bit Score: 45.67  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  53 YKEQTGEDIRIVyqtFDINEIMLTKI--EKGHEDFDVVC--PSEYIIerMLKKDLLLpidtvfphspdymndvSPYIREQ 128
Cdd:cd13544   20 FKKDTGIKVEFV---RLSTGEALARLeaEKGNPQADVWFggTADAHI--QAKKEGLL----------------EPYKSPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 129 IDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAE---SWSCLWDRKYAGKILMKD---SyrdayGTAiiYAHardL 202
Cdd:cd13544   79 ADKIPAKFKDPDGYWTGIYLGPLGFGVNTDELKEKGLPvpkSWEDLLNPEYKGEIVMPNpasS-----GTA--YTF---L 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 203 AggkvTVEDLMNDyspramEIAEKYLKAMKPNIAgweadfgkeMMTKN-KAWLNMTWSGDAKWAIEEADAV------GVD 275
Cdd:cd13544  149 A----SLIQLMGE------DEAWEYLKKLNKNVG---------QYTKSgSAPAKLVASGEAAIGISFLHDAlklkeqGYP 209

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 263256970 276 LDYVVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYV----SAVASPEIMEAKTDTTLTYYS 348
Cdd:cd13544  210 IKIIFPKEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYAiptnPDAKPPEIAPDLKKDKLIKYD 286
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 39-320 3.60e-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: 45.37  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  39 DYIGDGVLEDFqayyKEQTGEDIRIVyqTF-DINEiMLTKI--EKGHEDFDVVcpseyiiermlkkdllLPIDTVFPHSP 115
Cdd:cd13545   14 WGPGPEVKAEF----EKETGCKVEFV--KPgDAGE-LLNRLilEKNNPRADVV----------------LGLDNNLLSRA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 116 DYMNDVSPYIREQIDKL-SQPGRVASHYAVCYMWGTAGILYNKAFVPDADAeSWSCLWDRKYAGKILMKDSYRDAYGTAI 194
Cdd:cd13545   71 LKEGLFEPYRSPALDVVpEVPVFDPEDRLIPYDYGYLAFNYDKKKFKEPPL-SLEDLTAPEYKGLIVVQDPRTSSPGLGF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 195 IYAhardlaggkvtvedLMNDYSPramEIAEKYLKAMKPNI----AGWEADFGKEmmTKNKAWLNMTWSGDAKWAIEEAD 270
Cdd:cd13545  150 LLW--------------TIAVFGE---EGYLEYWKKLKANGvtvtPGWSEAYGLF--TTGEAPMVVSYATSPAYHVYYEK 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 263256970 271 avgvDLDY--VVPREGSNIWYDGWVIPKYAGNPEAASYFINFMCRP----DIALRN 320
Cdd:cd13545  211 ----DLRYtaVIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPefqeVIPETN 262
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 49-311 1.34e-04

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: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 43.37  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  49 FQAYYKEQTGEDIRiVYQ--TFDINEIMLTKIEKGHEDFDVVCPSE-YIIERMLKKDLLLPIDtvfphSPDymndvspyi 125
Cdd:cd13547   17 VEAFEKKYPGVKVE-VFRagTGKLMAKLAAEAEAGNPQADVLWVADpPTAEALKKEGLLLPYK-----SPE--------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 126 reqIDKLSQPGRVASHYAVCYMWGTAGILYNKAFVPDADAESWSCLWDRKYAGKILMKD-SYRdayGTAiiyahardlag 204
Cdd:cd13547   82 ---ADAIPAPFYDKDGYYYGTRLSAMGIAYNTDKVPEEAPKSWADLTKPKYKGQIVMPDpLYS---GAA----------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 205 gKVTVEDLMNDYspramEIAEKYLKAMKPNiagweadfGKEMMTKNKAWLNMTWSGDAKwaieeadaVGVDLDYVVPR-- 282
Cdd:cd13547  145 -LDLVAALADKY-----GLGWEYFEKLKEN--------GVKVEGGNGQVLDAVASGERP--------AGVGVDYNALRak 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 263256970 283 -EGS--NIWY--DGWV-------IPKYAGNPEAASYFINFM 311
Cdd:cd13547  203 eKGSplEVIYpeEGTVvipspiaILKGSKNPEAAKAFVDFL 243
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-311 2.59e-03

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 39.17  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970   45 VLEDFQAYYKEQTGEDIRIVYQtfdineimltkiekghedfdvvcPSEYIIERMLKKDlllPIDTVFPHSPDYMndvspy 124
Cdd:pfam13531  11 ALRELAAAFEAETGVKVVVSYG-----------------------GSGKLAKQIANGA---PADVFISADSAWL------ 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  125 ireqiDKLSQPGRVASHYAVCYMWGTAGILYNKAfvPDADAESWSCLWDRKYagKILMKDSYRDAYGTAiiyahardlag 204
Cdd:pfam13531  59 -----DKLAAAGLVVPGSRVPLAYSPLVIAVPKG--NPKDISGLADLLKPGV--RLAVADPKTAPSGRA----------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  205 gkvtvedlmndysprAMEIAEKY--LKAMKPNIAGWEADFGKEM--MTKNKAWLNMTWSGDAKWAieeadAVGVDLDYVV 280
Cdd:pfam13531 119 ---------------ALELLEKAglLKALEKKVVVLGENVRQALtaVASGEADAGIVYLSEALFP-----ENGPGLEVVP 178

                         250       260       270
                  ....*....|....*....|....*....|..
gi 263256970  281 PREGSNIWYD-GWVIPKYAGNPEAASYFINFM 311
Cdd:pfam13531 179 LPEDLNLPLDyPAAVLKKAAHPEAARAFLDFL 210
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 284-336 2.95e-03

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: 39.60  E-value: 2.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 263256970 284 GSNiwydgWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGY----VSAVASPEIM 336
Cdd:cd14747  273 GSN-----LAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMlpanTSAWDDPSLA 324
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-329 3.08e-03

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: 39.59  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  37 WADYIGDgvLEDFQAY---YKEQTGEDIRIVYQTF-DINEIMLTKIEKGHEDFDVVCPSEYIiERMLKKDLLLPIDTVFP 112
Cdd:cd13586    5 WTDEDGE--LEYLKELaeeFEKKYGIKVEVVYVDSgDTREKFITAGPAGKGPDVFFGPHDWL-GELAAAGLLAPIPEYLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 113 HSPDYmNDVSpyireqIDKLSQPGRVashYAVCYMWGTAGILYNKAFVPDAdAESW-------SCLWDRKYAGKILMKDs 185
Cdd:cd13586   82 VKIKN-LPVA------LAAVTYNGKL---YGVPVSVETIALFYNKDLVPEP-PKTWeelialaKKFNDKAGGKYGFAYD- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 186 YRDAYGTAIIYAhardLAGGKVTVED--------LMNDYSPRAMEIAEKYLKAMKPNIAGWEADFGKEMMTKNKAwlNMT 257
Cdd:cd13586  150 QTNPYFSYPFLA----AFGGYVFGENggdptdigLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKA--AMI 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 263256970 258 WSGDakWAIEEADAVGVDLDY-VVPREGSNIWYD------GWVIPKYAGNPEAASYFINFMCRPDIALRNMEASGYVSA 329
Cdd:cd13586  224 INGP--WDLADYKDAGINFGVaPLPTLPGGKQAApfvgvqGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPA 300
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 33-329 3.32e-03

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: 39.67  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970  33 KIYNWADYIG--DGVLEDFQAYYKEQTGED-IRIVY-QTFDINEIMLTKIEKGhEDFDVVCPSEYIIERMLKKDLLLPID 108
Cdd:cd13657    1 TITIWHALTGaeEDALQQIIDEFEAKYPVPnVKVPFeKKPDLQNKLLTAIPAG-EGPDLFIWAHDWIGQFAEAGLLVPIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 109 TVFphSPDYMNDvspYIREQIDKLSQPGRVashYAVCYMWGTAGILYNKAFVPDAD---AESWSCLWDRKY--AGKILMK 183
Cdd:cd13657   80 DYL--SEDDFEN---YLPTAVEAVTYKGKV---YGLPEAYETVALIYNKALVDQPPettDELLAIMKDHTDpaAGSYGLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 184 DSYRDAY-GTAIIYAhardlAGGKVTVEDLMNDY--SPrAMEIAEKYLKAMKPNIAGWEADFG--KEMMTKNKAwlNMTW 258
Cdd:cd13657  152 YQVSDAYfVSAWIFG-----FGGYYFDDETDKPGldTP-ETIKGIQFLKDFSWPYMPSDPSYNtqTSLFNEGKA--AMII 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 263256970 259 SGdaKWAIEEADAVGVDLDYVV-PREGSNIW------YDGWVIPKYA--GNPEAASYFINFMCRPDIALRNMEASGYVSA 329
Cdd:cd13657  224 NG--PWFIGGIKAAGIDLGVAPlPTVDGTNPprpysgVEGIYVTKYAerKNKEAALDFAKFFTTAEASKILADENGYVPA 301
 
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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