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Conserved domains on  [gi|953820509|ref|WP_058054127|]
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MULTISPECIES: ABC transporter substrate-binding protein [Aeromonas]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 6-325 6.47e-51

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 177.16  E-value: 6.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   6 IGALSLLLCG------QLMASELVIESWRTD--DKALWeQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGD 77
Cdd:COG1653   11 ALALALAACGgggsgaAAAAGKVTLTVWHTGggEAAAL-EALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  78 LITCrPFDDSLALFKAGHLAELTEMA-----GMENFPSFAQSPWQTDsGaQTFCVPMASVIHGFFYNKKIFSELGLTLPQ 152
Cdd:COG1653   90 VVQV-DSGWLAEFAAAGALVPLDDLLdddglDKDDFLPGALDAGTYD-G-KLYGVPFNTDTLGLYYNKDLFEKAGLDPPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 153 TRDQFFAVLDKIKADGRYVPLAMSGSESWVASELGFQNiGPNYWkGEDGRLAliggqerLDNPQYVKVFDELARWRS--Y 230
Cdd:COG1653  167 TWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLY-DEDGKPA-------FDSPEAVEALEFLKDLVKdgY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 231 LGEGGESRDYATSNELFTSGKAAFYVAGSWEIAPFT---GKVDFGVMRPPVAKQGDGCFFTDHTDiGMGMNPASKNKEGA 307
Cdd:COG1653  238 VPPGALGTDWDDARAAFASGKAAMMINGSWALGALKdaaPDFDVGVAPLPGGPGGKKPASVLGGS-GLAIPKGSKNPEAA 316

                        330
                 ....*....|....*...
gi 953820509 308 MAFLQWLTTPQFAELYTN 325
Cdd:COG1653  317 WKFLKFLTSPEAQAKWDA 334
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 6-325 6.47e-51

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 177.16  E-value: 6.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   6 IGALSLLLCG------QLMASELVIESWRTD--DKALWeQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGD 77
Cdd:COG1653   11 ALALALAACGgggsgaAAAAGKVTLTVWHTGggEAAAL-EALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  78 LITCrPFDDSLALFKAGHLAELTEMA-----GMENFPSFAQSPWQTDsGaQTFCVPMASVIHGFFYNKKIFSELGLTLPQ 152
Cdd:COG1653   90 VVQV-DSGWLAEFAAAGALVPLDDLLdddglDKDDFLPGALDAGTYD-G-KLYGVPFNTDTLGLYYNKDLFEKAGLDPPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 153 TRDQFFAVLDKIKADGRYVPLAMSGSESWVASELGFQNiGPNYWkGEDGRLAliggqerLDNPQYVKVFDELARWRS--Y 230
Cdd:COG1653  167 TWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLY-DEDGKPA-------FDSPEAVEALEFLKDLVKdgY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 231 LGEGGESRDYATSNELFTSGKAAFYVAGSWEIAPFT---GKVDFGVMRPPVAKQGDGCFFTDHTDiGMGMNPASKNKEGA 307
Cdd:COG1653  238 VPPGALGTDWDDARAAFASGKAAMMINGSWALGALKdaaPDFDVGVAPLPGGPGGKKPASVLGGS-GLAIPKGSKNPEAA 316

                        330
                 ....*....|....*...
gi 953820509 308 MAFLQWLTTPQFAELYTN 325
Cdd:COG1653  317 WKFLKFLTSPEAQAKWDA 334
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 21-399 1.12e-39

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


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 147.53  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  21 ELVIESWRT-DDKALWEQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGDLITCRPFDDSLALFKAGHLAEL 99
Cdd:cd14749    1 TITYWQYFTgDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 100 TEMAGME-----NFPSFAQSpwqTDSGAQTFCVPMASVIHGFFYNKKIFSELG-LTLPQTRDQFFAVLDKIKADGrYVPL 173
Cdd:cd14749   81 TDYLDPNgvdkrFLPGLADA---VTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKA-KGQT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 174 AMSGSESWVASELGFQNIGPNY---WKGEDGRlaligGQERLDNPQYVKVFDELA--RWRSYLGEGGESRDYATSNELFT 248
Cdd:cd14749  157 GFGLLLGAQGGHWYFQYLVRQAgggPLSDDGS-----GKATFNDPAFVQALQKLQdlVKAGAFQEGFEGIDYDDAGQAFA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 249 SGKAAFYVAGSWEIAPFTG---KVDFGVMRPPVAKQGDGCFFTDHTDIGMGMNPASKNKEGAMAFLQWLTTPQFAELYTN 325
Cdd:cd14749  232 QGKAAMNIGGSWDLGAIKAgepGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 326 --------------SLPGFFSLSNHFFDVTNPAAKEMmeWRDQcdstirvatqilsrGTPKLGDELAEVSQAVLLGKMEP 391
Cdd:cd14749  312 dvgllpakevvakdEDPDPVAILGPFADVLNAAGSTP--FLDE--------------YWPAAAQVHKDAVQKLLTGKIDP 375


                 ....*...
gi 953820509 392 KAAADRLE 399
Cdd:cd14749  376 EQVVKQAQ 383
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 29-318 3.31e-27

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: 110.97  E-value: 3.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   29 TDDKALweQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGG-KAGDLITCRPfDDSLALFKAGHLAELTEMAGMEN 107
Cdd:pfam01547   5 TEAAAL--QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGdGPADVFASDN-DWIAELAKAGLLLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  108 FPSFAQspwqtdsgaqTFCVPMASVIHGFFYNKKIFSELGLTLPQTRDQFFAVLDKIKADGRYVPLAMSGSESWVAS--- 184
Cdd:pfam01547  82 VLGVPK----------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyft 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  185 ELGFQNIGPNYWKGEDGRLALIGGQERLDNpqYVKVFDELARWRSYLGEGGESRDYATSNELFTSGKAAFYVAGSWEIAP 264
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITY--YVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 953820509  265 FTG--------------KVDFGVMRPPVAKQGDGcfftdhTDIGMGMNPASKNKEGAMAFLQWLTTPQ 318
Cdd:pfam01547 230 ANKvklkvafaapapdpKGDVGYAPLPAGKGGKG------GGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 6-325 6.47e-51

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 177.16  E-value: 6.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   6 IGALSLLLCG------QLMASELVIESWRTD--DKALWeQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGD 77
Cdd:COG1653   11 ALALALAACGgggsgaAAAAGKVTLTVWHTGggEAAAL-EALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  78 LITCrPFDDSLALFKAGHLAELTEMA-----GMENFPSFAQSPWQTDsGaQTFCVPMASVIHGFFYNKKIFSELGLTLPQ 152
Cdd:COG1653   90 VVQV-DSGWLAEFAAAGALVPLDDLLdddglDKDDFLPGALDAGTYD-G-KLYGVPFNTDTLGLYYNKDLFEKAGLDPPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 153 TRDQFFAVLDKIKADGRYVPLAMSGSESWVASELGFQNiGPNYWkGEDGRLAliggqerLDNPQYVKVFDELARWRS--Y 230
Cdd:COG1653  167 TWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLY-DEDGKPA-------FDSPEAVEALEFLKDLVKdgY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 231 LGEGGESRDYATSNELFTSGKAAFYVAGSWEIAPFT---GKVDFGVMRPPVAKQGDGCFFTDHTDiGMGMNPASKNKEGA 307
Cdd:COG1653  238 VPPGALGTDWDDARAAFASGKAAMMINGSWALGALKdaaPDFDVGVAPLPGGPGGKKPASVLGGS-GLAIPKGSKNPEAA 316

                        330
                 ....*....|....*...
gi 953820509 308 MAFLQWLTTPQFAELYTN 325
Cdd:COG1653  317 WKFLKFLTSPEAQAKWDA 334
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 21-399 1.12e-39

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


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 147.53  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  21 ELVIESWRT-DDKALWEQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGDLITCRPFDDSLALFKAGHLAEL 99
Cdd:cd14749    1 TITYWQYFTgDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 100 TEMAGME-----NFPSFAQSpwqTDSGAQTFCVPMASVIHGFFYNKKIFSELG-LTLPQTRDQFFAVLDKIKADGrYVPL 173
Cdd:cd14749   81 TDYLDPNgvdkrFLPGLADA---VTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKA-KGQT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 174 AMSGSESWVASELGFQNIGPNY---WKGEDGRlaligGQERLDNPQYVKVFDELA--RWRSYLGEGGESRDYATSNELFT 248
Cdd:cd14749  157 GFGLLLGAQGGHWYFQYLVRQAgggPLSDDGS-----GKATFNDPAFVQALQKLQdlVKAGAFQEGFEGIDYDDAGQAFA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 249 SGKAAFYVAGSWEIAPFTG---KVDFGVMRPPVAKQGDGCFFTDHTDIGMGMNPASKNKEGAMAFLQWLTTPQFAELYTN 325
Cdd:cd14749  232 QGKAAMNIGGSWDLGAIKAgepGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 326 --------------SLPGFFSLSNHFFDVTNPAAKEMmeWRDQcdstirvatqilsrGTPKLGDELAEVSQAVLLGKMEP 391
Cdd:cd14749  312 dvgllpakevvakdEDPDPVAILGPFADVLNAAGSTP--FLDE--------------YWPAAAQVHKDAVQKLLTGKIDP 375


                 ....*...
gi 953820509 392 KAAADRLE 399
Cdd:cd14749  376 EQVVKQAQ 383
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 35-399 1.97e-36

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: 138.31  E-value: 1.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  35 WEQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGDLITCRPFDdsLALF-KAGHLAELTE-MAGMENFPSFA 112
Cdd:cd13585   15 ALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPW--VPEFaSNGALLDLDDyIEKDGLDDDFP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 113 QSPWQTDS-GAQTFCVPMASVIHGFFYNKKIFSELGLTL--PQTRDQFF--AVLDKIKADGRYvPLAMSGSESWVA--SE 185
Cdd:cd13585   93 PGLLDAGTyDGKLYGLPFDADTLVLFYNKDLFDKAGPGPkpPWTWDELLeaAKKLTDKKGGQY-GFALRGGSGGQTqwYP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 186 LGFQNiGPNYWKGEDGRLAliggqerLDNPQYVKVFDELAR-WRSYLGEGGESRDYATSNELFTSGKAAFYVAGSWEIAP 264
Cdd:cd13585  172 FLWSN-GGDLLDEDDGKAT-------LNSPEAVEALQFYVDlYKDGVAPSSATTGGDEAVDLFASGKVAMMIDGPWALGT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 265 FTG---KVDFGVMRPPVAKQGDGCFFTdhTDIGMGMNPASKNKEGAMAFLQWLTTPQFAELYTNSLPGFFSLSNHFFDVT 341
Cdd:cd13585  244 LKDskvKFKWGVAPLPAGPGGKRASVL--GGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAA 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 342 NPAAKEMMEWRDQcDSTIRVATQILSRGTPKLGDELAEVSQAVLLGKME--PKAAADRLE 399
Cdd:cd13585  322 PDAKPALALAAAA-DALAAAVPPPVPPPWPEVYPILSEALQEALLGALGksPEEALKEAA 380
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 1.78e-32

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 128.14  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   1 MSKKWIGALSLLL--------CGQLMAS-----------ELVIesWRTDDKALWEQKIIPAFEAAhPGIKVSFHPVQNVN 61
Cdd:COG2182    1 MKRRLLAALALALalalalaaCGSGSSSsgsssaagaggTLTV--WVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  62 YMPTLWESLKGGKAGDLITCrPFDDSLALFKAGHLAELTE-MAGMENFPSFAQSPWQTDSgaQTFCVPMASVIHGFFYNK 140
Cdd:COG2182   78 LREKLTTAAPAGKGPDVFVG-AHDWLGELAEAGLLAPLDDdLADKDDFLPAALDAVTYDG--KLYGVPYAVETLALYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 141 KIFSElglTLPQTRDQFFAVLDKIKADGRYvPLAMSGSESWVASELGFQNiGPNYWKGEDGRLALIGgqerLDNPQYVKV 220
Cdd:COG2182  155 DLVKA---EPPKTWDELIAAAKKLTAAGKY-GLAYDAGDAYYFYPFLAAF-GGYLFGKDGDDPKDVG----LNSPGAVAA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 221 FDELARWRSYlGEGGESRDYATSNELFTSGKAAFYVAGSWEIAPFT--GKVDFGVMRPPVAKQGD------GCfftdhtd 292
Cdd:COG2182  226 LEYLKDLIKD-GVLPADADYDAADALFAEGKAAMIINGPWAAADLKkaLGIDYGVAPLPTLAGGKpakpfvGV------- 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 293 IGMGMNPASKNKEGAMAFLQWLTTPQFAELYtnslpgffslsnhfFDVTN--PAAKEMME-WRDQCDSTIRVATQILSRG 369
Cdd:COG2182  298 KGFGVSAYSKNKEAAQEFAEYLTSPEAQKAL--------------FEATGriPANKAAAEdAEVKADPLIAAFAEQAEYA 363

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 953820509 370 -----TPKLG---DELAEVSQAVLLGKMEPKAAAD 396
Cdd:COG2182  364 vpmpnIPEMGavwTPLGTALQAIASGKADPAEALD 398
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 37-399 6.65e-28

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: 114.70  E-value: 6.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  37 QKIIPAFEAAHPGIKVSfhpVQNVNYMPTLWE----SLKGGKAGDLITCrpFDDSLALF-KAGHLAELTEMAGMENF--P 109
Cdd:cd14748   17 EELVDEFNKSHPDIKVK---AVYQGSYDDTLTkllaALAAGTAPDVAQV--DASWVAQLaDSGALEPLDDYIDKDGVddD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 110 SFAQSPWQ--TDSGaQTFCVPMASVIHGFFYNKKIFSELGL---TLPQTRDQFFAVLDKIKADGR---YVPLAM-SGSES 180
Cdd:cd14748   92 DFYPAALDagTYDG-KLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGktgRYGFALpPGDGG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 181 WVASELGFQNiGPNYWKGEDGRLALiggqerlDNPQYVKVFDElarWRSYLGEGGESR--DYATSNELFTSGKAAFYVAG 258
Cdd:cd14748  171 WTFQALLWQN-GGDLLDEDGGKVTF-------NSPEGVEALEF---LVDLVGKDGVSPlnDWGDAQDAFISGKVAMTING 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 259 SWEIAPF---TGKVDFGVMRPPVAKQGDGCFFTDHTDIGMgMNPASKNKEGAMAFLQWLTTPQFAelytnslpGFFSLSN 335
Cdd:cd14748  240 TWSLAGIrdkGAGFEYGVAPLPAGKGKKGATPAGGASLVI-PKGSSKKKEAAWEFIKFLTSPENQ--------AKWAKAT 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953820509 336 HFFDVTNPAAKEMMEWRDQcDSTIRVATQILSRGTPKLG---------DELAEVSQAVLLGKMEPKAAADRLE 399
Cdd:cd14748  311 GYLPVRKSAAEDPEEFLAE-NPNYKVAVDQLDYAKPWGPpvpngaeirDELNEALEAALLGKKTPEEALKEAQ 382
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 29-318 3.31e-27

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: 110.97  E-value: 3.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   29 TDDKALweQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGG-KAGDLITCRPfDDSLALFKAGHLAELTEMAGMEN 107
Cdd:pfam01547   5 TEAAAL--QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGdGPADVFASDN-DWIAELAKAGLLLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  108 FPSFAQspwqtdsgaqTFCVPMASVIHGFFYNKKIFSELGLTLPQTRDQFFAVLDKIKADGRYVPLAMSGSESWVAS--- 184
Cdd:pfam01547  82 VLGVPK----------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyft 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  185 ELGFQNIGPNYWKGEDGRLALIGGQERLDNpqYVKVFDELARWRSYLGEGGESRDYATSNELFTSGKAAFYVAGSWEIAP 264
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITY--YVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 953820509  265 FTG--------------KVDFGVMRPPVAKQGDGcfftdhTDIGMGMNPASKNKEGAMAFLQWLTTPQ 318
Cdd:pfam01547 230 ANKvklkvafaapapdpKGDVGYAPLPAGKGGKG------GGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 21-399 1.16e-25

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: 107.77  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  21 ELVIESWRTDDKAlWEQKIIPAFEAAHpGIKVSFHPVQNVNYMPTLWESLKGGKAGDLITCrPFDDSLALFKAGHLAELT 100
Cdd:cd13586    1 TITVWTDEDGELE-YLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFG-PHDWLGELAAAGLLAPIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 101 EMAGMENFpsFAQSPWQTDS-GAQTFCVPMASVIHGFFYNKKIFSELgltlPQTRDQFFAVLDKI-KADGRYVPLAMSGS 178
Cdd:cd13586   78 EYLAVKIK--NLPVALAAVTyNGKLYGVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFnDKAGGKYGFAYDQT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 179 ESWVASELgFQNIGPNYWKGEDGRLALIGgqerLDNPQYVKVFDELARWRSYLGEGGESRDYATSNELFTSGKAAFYVAG 258
Cdd:cd13586  152 NPYFSYPF-LAAFGGYVFGENGGDPTDIG----LNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIING 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 259 SWEIAPF-TGKVDFGVMRPPVAKQGDG--CFFTDhtdIGMGMNPASKNKEGAMAFLQWLTTPQFAELytnslpgffslsn 335
Cdd:cd13586  227 PWDLADYkDAGINFGVAPLPTLPGGKQaaPFVGV---QGAFVSAYSKNKEAAVEFAEYLTSDEAQLL------------- 290

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 953820509 336 hFFDVTN--PAAKEMMEWRDQCDSTIRVA-TQILSRGTP--------KLGDELAEVSQAVLLGKMEPKAAADRLE 399
Cdd:cd13586  291 -LFEKTGriPALKDALNDAAVKNDPLVKAfAEQAQYGVPmpnipemaAVWDAMGNALNLVASGKATPEEAAKDAV 364
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 24-399 4.31e-21

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


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 94.75  E-value: 4.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  24 IESWRT---DDKALWeQKIIPAFEAAHPGIKVsfhpvqNVNYMPtlWESLK--------GGKAGDLITCrpfdDS--LAL 90
Cdd:cd14751    2 ITFWHTssdEEKVLY-EKLIPAFEKEYPKIKV------KAVRVP--FDGLHnqiktaaaGGQAPDVMRA----DIawVPE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  91 F-KAGHLAELTEMAGMENFPSFAQSPWQTDS-GAQTFCVPMASVIHGFFYNKKIFSELGLTLPQTRDQFFAVLDKI-KAD 167
Cdd:cd14751   69 FaKLGYLQPLDGTPAFDDIVDYLPGPMETNRyNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIkKKK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 168 GRYVpLAMSGSESWvaselgfqNIGPNYWkGEDGrlALIGGQER---LDNPQYVKVFDELARW-RSYLGEGGESRDYATS 243
Cdd:cd14751  149 GRYG-LYISGDGPY--------WLLPFLW-SFGG--DLTDEKKAtgyLNSPESVRALETIVDLyDEGAITPCASGGYPNM 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 244 NELFTSGKAAFYVAGSWEIA------PFTGKVDFGVMRPPVAKQGDGCFFTDHTdigMGMNPASKNKEGAMAFLQWLTTP 317
Cdd:cd14751  217 QDGFKSGRYAMIVNGPWAYAdilggkEFKDPDNLGIAPVPAGPGGSGSPVGGED---LVIFKGSKNKDAAWKFVKFMSSA 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 318 QFAELYT---NSLPgffslsnhffdvTNPAAKEMMEWRDqcDSTIRVATQILSRGTP--------KLGDELAEVSQAVLL 386
Cdd:cd14751  294 EAQALTAaklGLLP------------TRTSAYESPEVAN--NPMVAAFKPALETAVPrppipewgELFEPLTLAFAKVLR 359

                        410
                 ....*....|...
gi 953820509 387 GKMEPKAAADRLE 399
Cdd:cd14751  360 GEKSPREALDEAA 372
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-400 1.42e-17

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


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 84.00  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  37 QKIIPAFEAAHPGIKVsfhpvqNVNYMPTLWESLK------GGKAGDLITcRPFDDSLALFKAGHLAELTEMAGMENFps 110
Cdd:cd13522   17 NELIAKFEKAYPGITV------EVTYQDTEARRQFfstaaaGGKGPDVVF-GPSDSLGPFAAAGLLAPLDEYVSKSGK-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 111 FAQSPWQTDS-GAQTFCVPMASVIHGFFYNKKIFSElglTLPQTRDQFFAVLDKIKADGRYvPLAMSGSE-----SWVAS 184
Cdd:cd13522   88 YAPNTIAAMKlNGKLYGVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAKNVW-GLVYNQNEpyffaAWIGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 185 eLGFQNIGPNYWKGEDGrlaliggqerLDNPQYVKVFDELARWRSYLGEGGESRDYATSNELFTSGKAAFYVAGSWEIAP 264
Cdd:cd13522  164 -FGGQVFKANNGKNNPT----------LDTPGAVEALQFLVDLKSKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 265 F--TGKVDFGVMRPPVAKQGDGCF-FTDHTdiGMGMNPASKNKEGAMAFLQWLTTPQFAELY---TNSLPGFFSLSNHFF 338
Cdd:cd13522  233 YrqALKINLGVAPLPTFSGTKHAApFVGGK--GFGINKESQNKAAAVEFVKYLTSYQAQLVLfddAGDIPANLQAYESPA 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 339 DVTNPAAKEMMEwrdqcdstirvatqILSRGTPK--------LGDELAEVSQAVLLGKMEPKAAADRLEG 400
Cdd:cd13522  311 VQNKPAQKASAE--------------QAAYGVPMpnipemraVWDAFRIAVNSVLAGKVTPEAAAKDAQQ 366
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 38-324 3.25e-16

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 78.99  E-value: 3.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509   38 KIIPAFEAAHpGIKVSFHPVQNVNYMPTLWESLKGGKAGDL-ITCRPFDDSLALFKAGHLAELTEMAGMENFPSFAqSPW 116
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLdVVWIAADQLATLAEAGLLADLSDVDNLDDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  117 QTDsgAQTFCVP-MASVIHGFFYNKKIFSELGLTlPQTRDQFFAVLDKIKadGRYVpLAMSGSESWVAselgfqnigpny 195
Cdd:pfam13416  79 GYD--GKLYGVPyAASTPTVLYYNKDLLKKAGED-PKTWDELLAAAAKLK--GKTG-LTDPATGWLLW------------ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  196 wkgedgrLALIGGQerlDNPQYVKVFDELARWRSYLGEGGES----RDYATSNELFTSGKAAFYVAGSWEIAPFT-GKVD 270
Cdd:pfam13416 141 -------ALLADGV---DLTDDGKGVEALDEALAYLKKLKDNgkvyNTGADAVQLFANGEVAMTVNGTWAAAAAKkAGKK 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 953820509  271 FGVMRPpvaKQGdgcFFTDHTdiGMGMNPASKNKE-GAMAFLQWLTTP-QFAELYT 324
Cdd:pfam13416 211 LGAVVP---KDG---SFLGGK--GLVVPAGAKDPRlAALDFIKFLTSPeNQAALAE 258
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 27-329 1.14e-15

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: 78.51  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  27 WRTDD--KALWEQKIIPAFEAAHPGIKVSFHPVQNVNYMPTLWESLKGGKAGDLI----TcrpfddSLALF-KAGHLAEL 99
Cdd:cd14747    5 WAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVqlgnT------WVAEFaAMGALEDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 100 T----EMAGMENFPsfaqsPWQTDSG---AQTFCVPMASVIHGFFYNKKIFSELG-LTLPQTRDQFFAVLDKIKADG-RY 170
Cdd:cd14747   79 TpyleDLGGDKDLF-----PGLVDTGtvdGKYYGVPWYADTRALFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGpDV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 171 VPLAMSGSESWvaselgFQNIGPNYWkGEDGRLAL-IGGQERLDNPQYVKVFDElarWRSYLGEG--GESRDYATSN--E 245
Cdd:cd14747  154 SGFAIPGKNDV------WHNALPFVW-GAGGDLATkDKWKATLDSPEAVAGLEF---YTSLYQKGlsPKSTLENSADveQ 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 246 LFTSGKAAFYVAGSWEIAPFT-------GKVDFGVMrPPVAKQGDGCFFtdhtdiG---MGMNPASKNKEGAMAFLQWLT 315
Cdd:cd14747  224 AFANGKVAMIISGPWEIGAIReagpdlaGKWGVAPL-PGGPGGGSPSFA------GgsnLAVFKGSKNKDLAWKFIEFLS 296

                        330
                 ....*....|....*..
gi 953820509 316 TPQFAELY---TNSLPG 329
Cdd:cd14747  297 SPENQAAYakaTGMLPA 313
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 37-317 2.78e-15

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: 77.03  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  37 QKIIPAFEAAHPGIKVsfhpvqNVNY--MPTLWESLKG----GKAGDLITCRpfDDSLALF-KAGHLAELTEMAG---ME 106
Cdd:cd13657   17 QQIIDEFEAKYPVPNV------KVPFekKPDLQNKLLTaipaGEGPDLFIWA--HDWIGQFaEAGLLVPISDYLSeddFE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 107 NFPSFAQSPWQTDsgAQTFCVPMASVIHGFFYNKKIFSELgltlPQTRDQFFAVLDKI--KADGRYvPLAMSGSESWVAS 184
Cdd:cd13657   89 NYLPTAVEAVTYK--GKVYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHtdPAAGSY-GLAYQVSDAYFVS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 185 ELgFQNIGPNYWKGEDGRLALiggqerlDNPQYVKVFDELARW-RSYLGEGGesrDYATSNELFTSGKAAFYVAGSWEIA 263
Cdd:cd13657  162 AW-IFGFGGYYFDDETDKPGL-------DTPETIKGIQFLKDFsWPYMPSDP---SYNTQTSLFNEGKAAMIINGPWFIG 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 953820509 264 PFT-GKVDFGVMR-PPVAKQGDGCFFTDHTDIGMGMNPASKNKEGAMAFLQWLTTP 317
Cdd:cd13657  231 GIKaAGIDLGVAPlPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTA 286
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 30-396 3.74e-14

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


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 73.67  E-value: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  30 DDKALWEQKIIPAFEAAHpGIKVSFHPVQNVNYMPTLweSLKG--GKAGDLITCrPFDDSLALFKAGHLAELTEMAGmEN 107
Cdd:cd13658    9 DKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKL--SLDGpaGKGPDVMVA-PHDRIGSAVLQGLLSPIKLSKD-KK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 108 FPSFAQSPWQTDSGAQTFCVPMASVIHGFFYNKKIFSELgltlPQTRDQFFAVLDKI--KADGRYVPLAmsgseSWVASE 185
Cdd:cd13658   84 KGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLtkEKGKQYGFLA-----DATNFY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 186 LGFQNIGPN--YWKGEDGRLALIGgQERLDNPQYVKVFDELARWRS--YLGEGGESRdyaTSNELFTSGKAAFYVAGSWE 261
Cdd:cd13658  155 YSYGLLAGNggYIFKKNGSDLDIN-DIGLNSPGAVKAVKFLKKWYTegYLPKGMTGD---VIQGLFKEGKAAAVIDGPWA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 262 IAPF-TGKVDFGVmrPPVAKQGDGCFFtdHTDIGMG---MNPASKNKEGAMAFLQWLTTPQFAELYtnslpgffslsnhf 337
Cdd:cd13658  231 IQEYqEAGVNYGV--APLPTLPNGKPM--APFLGVKgwyLSAYSKHKEWAQKFMEFLTSKENLKKR-------------- 292

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 338 FDVTN--PAAKEMMEWRD-QCDSTIRVATQILSRGTPKLG-DELAEV-------SQAVLLGKMEPKAAAD 396
Cdd:cd13658  293 YDETNeiPPRKDVRSDPEiKNNPLTSAFAKQASRAVPMPNiPEMGAVwepannaLFFILSGKKTPKQALN 362
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 35-317 3.11e-11

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


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 65.01  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  35 WEQKIIPAFEAAHPGIKVSFHPVQN-----VNYMPTLWESlkGGKAGDLITcrpFDDS-LALF-KAGHLAELTEMAGMEN 107
Cdd:cd14750   15 LLKKAIAAFEKKHPDIKVEIEELPAssddqRQQLVTALAA--GSSAPDVLG---LDVIwIPEFaEAGWLLPLTEYLKEEE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 108 FPSFAQSPWQTDS-GAQTFCVPMASVIHGFFYNKKIFSELGLTLPQTRDQFFAV-LDKIKADGRYVPLAMSGSEswvaSE 185
Cdd:cd14750   90 DDDFLPATVEANTyDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAaKKRKAGEPGIWGYVFQGKQ----YE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 186 LGFQNIGPNYWKGEDGRLALIGGQERLDNPQYVKVFDELARWRSY-------LGEGGESrdyatSNELFTSGKAAFyvAG 258
Cdd:cd14750  166 GLVCNFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEgispkgvLTYGEEE-----ARAAFQAGKAAF--MR 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953820509 259 SW---------EIAPFTGKVDFGvmrPPVAKQGDGcfftDHTDIG---MGMNPASKNKEGAMAFLQWLTTP 317
Cdd:cd14750  239 NWpyayallqgPESAVAGKVGVA---PLPAGPGGG----SASTLGgwnLAISANSKHKEAAWEFVKFLTSP 302
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 135-329 8.02e-07

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


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 51.30  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 135 GFFYNKKIFSELGLTLPQTRDQFFAVLDKIKADG--------RYVPLAMSGSESW---VASELGFQNIGPNY--WKGEDG 201
Cdd:cd13521  128 GYFIRKDWLDKLNLKTPKTLDELYNVLKAFKEKDpngngkadEIPFIDRDPLYGAfrlINSWGARSAGGSTDsdWYEDNG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 202 RLALIGGQErldnpQYVKVFDELARWRSylgEG---GES--RDYATSNELFTSGKAAFYVAGSWEI-APFT---GKVDFG 272
Cdd:cd13521  208 KFKHPFASE-----EYKDGMKYMNKLYT---EGlidKESftQKDDQAEQKFSNGKLGGFTHNWFASdNLFTaqlGKEKPM 279

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953820509 273 VMRPPVAKQGDGCFFTDHTDIGMGMNPA------SKNKEGAMAFLQWLTTPQFAELYTNSLPG 329
Cdd:cd13521  280 YILLPIAPAGNVKGRREEDSPGYTGPDGvaiskkAKNPVAALKFFDWLASEEGRELANFGIEG 342
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-329 7.72e-06

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 48.09  E-value: 7.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  73 GKAGDLITCRPFDDSLALFKAGHLAELTEMAGmENFPSFAQSPWQTDSGAQTF-----CVPMASVI---HGFFYNKKIFS 144
Cdd:cd13580   57 GDLPDIVVVNDPQLSITLVKQGALWDLTDYLD-KYYPNLKKIIEQEGWDSASVdgkiyGIPRKRPLigrNGLWIRKDWLD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 145 ELGLTLPQTRDQFFAVLDKIK---ADGRYVPL---AMSGSESWVASELGFQNI----GPNYWKGEDGRLALIGGQerldn 214
Cdd:cd13580  136 KLGLEVPKTLDELYEVAKAFTekdPDGNGKKDtygLTDTKDLIGSGFTGLFGAfgapPNNWWKDEDGKLVPGSIQ----- 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 215 PQYVKVFDELARWRSylgEGGESRDYAT-----SNELFTSGKAAFYVAGSWEIAPFTGKVDFGVmrpPVAKQGD-GCFFT 288
Cdd:cd13580  211 PEMKEALKFLKKLYK---EGLIDPEFAVndgtkANEKFISGKAGIFVGNWWDPAWPQASLKKND---PDAEWVAvPIPSG 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 953820509 289 DHTDIGMGMNPA----------SKNKEGAMAFLQWLTTPQFAELYTNSLPG 329
Cdd:cd13580  285 PDGKYGVWAESGvngffvipkkSKKPEAILKLLDFLSDPEVQKLLDYGIEG 335
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 27-316 1.01e-05

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


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 47.73  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  27 WRTDDKALWEQKIIPAFEAAHPGIKVSFHPVQNvnymptlweslKGGKAGDLITCRP------F---DDSL-ALFKAGHL 96
Cdd:cd13655    5 WGPQEDQEWLKEMVDAFKEKHPEWKITITIGVV-----------GEADAKDEVLKDPsaaadvFafaNDQLgELVDAGAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509  97 AELTemagmenfPSFAQSPWQTDS----GAQT-----FCVPMASVIHGFFYNKKIFSELGLtlpQTRDQffaVLDKIKAD 167
Cdd:cd13655   74 YPLT--------GSAVDKIKNTNSeatvDAVTyngklYGYPFTANTWFMYYDKSKLTEDDV---KSLDT---MLAKAPDA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 168 GRYVplAMSGSESWVASELGFQNIG---------PNY--WKGEDGRLALIGGQERLDNPQYVKVFDELARwrsylgegge 236
Cdd:cd13655  140 KGKV--SFDLSNSWYLYAFFFGAGCklfgnnggdTAGcdFNNEKGVAVTNYLVDLVANPKFVNDADGDAI---------- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 237 srdyatsnELFTSGKAAFYVAGSWEIAPFTGKV--DFGVMRPPVAKqgdgcffTDHTDI---------GMGMNPASKNKE 305
Cdd:cd13655  208 --------SGLKDGTLGAGVSGPWDAANLKKALgdNYAVAKLPTYT-------LGGKDVqmksfagykAIGVNSNTKNPE 272

                        330
                 ....*....|.
gi 953820509 306 GAMAFLQWLTT 316
Cdd:cd13655  273 AAMALADYLTN 283
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 134-324 1.22e-05

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 47.74  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 134 HGFFYNKKIFSELGLTLPQTRDQFFAVLDKIK-ADGRYVPLAMSGSES----WVASELGFQNIGPN---YWKGEDGRLAL 205
Cdd:cd13583  128 YSFLYRKDIFEKAGIKIPTTWDEFYAALKKLKeKYPDSYPYSDRWNSNalllIAAPAFGTTAGWGFsnyTYDPDTDKFVY 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953820509 206 IGGQErlDNPQYVKVFDELarwrsyLGEGGESRDYATS-----NELFTSGKAAFYVAGSWEIAPF------TGKVDFGVM 274
Cdd:cd13583  208 GATTD--EYKDMLQYFNKL------YAEGLLDPESFTQtddqaKAKFLNGKSFVITTNPQTVDELqrnlraADGGNYEVV 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 953820509 275 R--PPVAKQGDGcFFTDHTDIGMGMNPA---SKNKEGAMAFLQWLTTPQFAELYT 324
Cdd:cd13583  280 SitPPAGPAGKA-INGSRLENGFMISSKakdSKNFEALLQFLDWLYSDEGQELAT 333
PBP2_FutA1_ilke cd13542
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ...
 272-324 5.45e-03

Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic binding fold superfamily; FutA1 is the periplasmic component of an ABC-type iron transporter and serves as the primary receptor in Synerchosystis species. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria and is critical for survival of these pathogens within the host. After binding iron with high affinity, FutA1 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: 270260 [Multi-domain]  Cd Length: 314  Bit Score: 38.86  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 953820509 272 GVMRPPVAKQGDgcfftdHTDI-GMGMNPASKNKEGAMAFLQWLTTPQFAELYT 324
Cdd:cd13542  217 GVFFPNQDNRGT------HVNIsGIGVTKYAKNKENAIKFLEFLVSEPAQKLYA 264
 
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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