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Conserved domains on  [gi|1751874397|dbj|BBN96656|]
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ABC transporter substrate-binding protein (plasmid) [Deinococcus grandis]

Protein Classification

sugar ABC transporter substrate-binding protein( domain architecture ID 10194401)

sugar ABC transporter substrate-binding protein functions as the initial receptor in the active transport of sugars

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-412 6.43e-54

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: 183.76  E-value: 6.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAAA--KALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFT 101
Cdd:cd13585     1 TLTFWDWGQPAetAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAG--TAPDVFYVDGPWVPEFASN--GALL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNTLGAN-KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTAIKTWDDFIAAGKKVNAKFGGKVK 180
Cdd:cd13585    77 DLDDYIEKdGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVV---MTSDWGGQITAFKANRLASAMF 257
Cdd:cd13585   157 FALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVApssATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 258 GAWYEGTIRTNAADqsGKWGVYPMPASKAGGvRASNLGGSALALPSSSKNKAAAYAFMEnaLATTNGQVTMLRSQGLVPS 337
Cdd:cd13585   237 GPWALGTLKDSKVK--FKWGVAPLPAGPGGK-RASVLGGWGLAISKNSKHPEAAWKFIK--FLTSKENQLKLGGAAGPAA 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 338 LLTASKDAYVNQKQPYWGNQTVWKTILDTLGDVPAARGTQYFQDARQVMIVVQADYIKgkyKTAQDALNDAAKKI 412
Cdd:cd13585   312 LAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALG---KSPEEALKEAAKEI 383
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-412 6.43e-54

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: 183.76  E-value: 6.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAAA--KALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFT 101
Cdd:cd13585     1 TLTFWDWGQPAetAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAG--TAPDVFYVDGPWVPEFASN--GALL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNTLGAN-KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTAIKTWDDFIAAGKKVNAKFGGKVK 180
Cdd:cd13585    77 DLDDYIEKdGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVV---MTSDWGGQITAFKANRLASAMF 257
Cdd:cd13585   157 FALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVApssATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 258 GAWYEGTIRTNAADqsGKWGVYPMPASKAGGvRASNLGGSALALPSSSKNKAAAYAFMEnaLATTNGQVTMLRSQGLVPS 337
Cdd:cd13585   237 GPWALGTLKDSKVK--FKWGVAPLPAGPGGK-RASVLGGWGLAISKNSKHPEAAWKFIK--FLTSKENQLKLGGAAGPAA 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 338 LLTASKDAYVNQKQPYWGNQTVWKTILDTLGDVPAARGTQYFQDARQVMIVVQADYIKgkyKTAQDALNDAAKKI 412
Cdd:cd13585   312 LAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALG---KSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 24-328 3.52e-47

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 165.60  E-value: 3.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAA-AKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFTD 102
Cdd:COG1653    34 TLTVWHTGGGeAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAG--NAPDVVQVDSGWLAEFAAA--GALVP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 103 LNTL--GANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTaiKTWDDFIAAGKKVNAKfggKVK 180
Cdd:COG1653   110 LDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKAK---DGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYFDNtASQITIAKSGCVQALDTVKKLFANDVV----MTSDWGGQITAFKANRLASAM 256
Cdd:COG1653   185 YGFALGGKDGAAWLDLLLSAGGDLYDE-DGKPAFDSPEAVEALEFLKDLVKDGYVppgaLGTDWDDARAAFASGKAAMMI 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751874397 257 FGAWYEGTIRTNAADQsgKWGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMEnALATTNGQVTM 328
Cdd:COG1653   264 NGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKW 332
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 32-319 1.03e-18

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: 85.93  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  32 AAAKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGGADmPDVYSIENNEAEVFWARfpDCFTDLNTLGANKY 111
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGP-ADVFASDNDWIAELAKA--GLLLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 112 AKSFPafkwteltvgnKRYAMPWDSGPVVIFYRRDLYQQAGVNPtaIKTWDDFIAAGKKVNAKFGGKVKMGAIGNGQDDE 191
Cdd:pfam01547  82 VLGVP-----------KLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 192 WF-RMLANQNGCFYFD-------NTASQITIAKSGCVQALDTVKKLFANDVVMTSDWGGQITAFKANRLASAMFGAWYEG 263
Cdd:pfam01547 149 YFtLALLASLGGPLFDkdgggldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 264 TIRT---------NAADQSGKWGVYPMPASKAGGVrasnlGGSALALPSSSKNKAAAYAFMENAL 319
Cdd:pfam01547 229 AANKvklkvafaaPAPDPKGDVGYAPLPAGKGGKG-----GGYGLAIPKGSKNKEAAKKFLDFLT 288
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
110-324 2.25e-05

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 46.16  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 110 KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFIAAGKKVNAKfgGKvkmGAIGNGQD 189
Cdd:PRK09474  110 AFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLV------PTPPKTWEEIPALDKELKAK--GK---SAIMWNLQ 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 190 DEWFR--MLANQNG-CFYFDN---TASQITIAKSGCVQALDTVKKLFANDVV-MTSDWGGQITAFKANRLASAMFGAWYE 262
Cdd:PRK09474  179 EPYFTwpLIAADGGyAFKFENggyDVKDVGVNNAGAKAGLQFLVDLVKNKHMnADTDYSIAEAAFNKGETAMTINGPWAW 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751874397 263 GTIrtnaaDQSG-KWGVYPMPASKAGGVRASnLGGSALALPSSSKNKAAAYAFMENALATTNG 324
Cdd:PRK09474  259 SNI-----DKSGiNYGVTVLPTFNGKPSKPF-VGVLSAGINAASPNKELAKEFLENYLLTDEG 315
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-412 6.43e-54

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: 183.76  E-value: 6.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAAA--KALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFT 101
Cdd:cd13585     1 TLTFWDWGQPAetAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAG--TAPDVFYVDGPWVPEFASN--GALL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNTLGAN-KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTAIKTWDDFIAAGKKVNAKFGGKVK 180
Cdd:cd13585    77 DLDDYIEKdGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVV---MTSDWGGQITAFKANRLASAMF 257
Cdd:cd13585   157 FALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVApssATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 258 GAWYEGTIRTNAADqsGKWGVYPMPASKAGGvRASNLGGSALALPSSSKNKAAAYAFMEnaLATTNGQVTMLRSQGLVPS 337
Cdd:cd13585   237 GPWALGTLKDSKVK--FKWGVAPLPAGPGGK-RASVLGGWGLAISKNSKHPEAAWKFIK--FLTSKENQLKLGGAAGPAA 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 338 LLTASKDAYVNQKQPYWGNQTVWKTILDTLGDVPAARGTQYFQDARQVMIVVQADYIKgkyKTAQDALNDAAKKI 412
Cdd:cd13585   312 LAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALG---KSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 24-328 3.52e-47

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 165.60  E-value: 3.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAA-AKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFTD 102
Cdd:COG1653    34 TLTVWHTGGGeAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAG--NAPDVVQVDSGWLAEFAAA--GALVP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 103 LNTL--GANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTaiKTWDDFIAAGKKVNAKfggKVK 180
Cdd:COG1653   110 LDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKAK---DGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYFDNtASQITIAKSGCVQALDTVKKLFANDVV----MTSDWGGQITAFKANRLASAM 256
Cdd:COG1653   185 YGFALGGKDGAAWLDLLLSAGGDLYDE-DGKPAFDSPEAVEALEFLKDLVKDGYVppgaLGTDWDDARAAFASGKAAMMI 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751874397 257 FGAWYEGTIRTNAADQsgKWGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMEnALATTNGQVTM 328
Cdd:COG1653   264 NGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKW 332
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 24-412 3.69e-44

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: 158.22  E-value: 3.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSW--DAAAKALESTIPSFNKKYPNVKVNVVDLGNQNvYDRGLAGCAAGGADMPDVYSIENNEAEVFWARFPdcFT 101
Cdd:cd14748     1 EITFWHGmsGPDGKALEELVDEFNKSHPDIKVKAVYQGSYD-DTLTKLLAALAAGTAPDVAQVDASWVAQLADSGA--LE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNTL--GANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNP-TAIKTWDDFIAAGKKVNAKFGGK 178
Cdd:cd14748    78 PLDDYidKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPeKPPKTWDELEEAAKKLKDKGGKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 179 VKMG-AIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVVMTS-DWGGQITAFKANRLASAM 256
Cdd:cd14748   158 GRYGfALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLnDWGDAQDAFISGKVAMTI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 257 FGAWYEGTIRTNAADqsGKWGVYPMPAsKAGGVRASNLGGSALALPS-SSKNKAAAYAFMEnALATTNGQVTMLRSQGLV 335
Cdd:cd14748   238 NGTWSLAGIRDKGAG--FEYGVAPLPA-GKGKKGATPAGGASLVIPKgSSKKKEAAWEFIK-FLTSPENQAKWAKATGYL 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751874397 336 PslltASKDAYVNQKQpYWGNQTVWKTILDTLGDVPAARG-TQYFQDARQVMIVVQADYIKGKyKTAQDALNDAAKKI 412
Cdd:cd14748   314 P----VRKSAAEDPEE-FLAENPNYKVAVDQLDYAKPWGPpVPNGAEIRDELNEALEAALLGK-KTPEEALKEAQEKI 385
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 24-412 2.95e-40

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


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 147.46  E-value: 2.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSW--DAAAKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENNEAEVFWARfpDCFT 101
Cdd:cd14747     1 TLTVWAMgnSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASG--DGPDVVQLGNTWVAEFAAM--GALE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNT-LGANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNpTAIKTWDDFIAAGKKVNAKFGGKVK 180
Cdd:cd14747    77 DLTPyLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGD-EAPKTWDELEAAAKKIKADGPDVSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 181 MGAIGNGQDDEWFRMLANQNGCFYF--DNTASQITIAKSgcVQALDTVKKLFAN---DVVMTSDWGGQITAFKANRLASA 255
Cdd:cd14747   156 FAIPGKNDVWHNALPFVWGAGGDLAtkDKWKATLDSPEA--VAGLEFYTSLYQKglsPKSTLENSADVEQAFANGKVAMI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 256 MFGAWYEGTIRTNAADQSGKWGVYPMPAsKAGGVRASNLGGSALALPSSSKNKAAAYAFMEnALATTNGQVTMLRSQGLV 335
Cdd:cd14747   234 ISGPWEIGAIREAGPDLAGKWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKATGML 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751874397 336 PSLLTASKDAYVNQKQPYwgnqTVWKTILDTLGDVPAARGtqyFQDARQVMIVVQADYIKGKYKTAQDALNDAAKKI 412
Cdd:cd14747   312 PANTSAWDDPSLANDPLL----AVFAEQLKTGKATPATPE---WGEIEAELVLVLEEVWIGVGADVEDALDKAAAEI 381
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
23-415 1.43e-34

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 132.77  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  23 GTVTVWSWDAAAKALESTIPSFNKKyPNVKVNVVDLGNQNVYDRGLAGCAAGgaDMPDVYSIENneaevfwarfpdcfTD 102
Cdd:COG2182    39 GTLTVWVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAG--KGPDVFVGAH--------------DW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 103 LNTLGAN----------KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLyqqagVNPTAIKTWDDFIAAGKKVN 172
Cdd:COG2182   102 LGELAEAgllapldddlADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDL-----VKAEPPKTWDELIAAAKKLT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 173 AKfggkvKMGAIGNGQDDEWFRM-LANQNGCFYFDNTA---SQITIAKSGCVQALDTVKKLFANDVVMTS-DWGGQITAF 247
Cdd:COG2182   177 AA-----GKYGLAYDAGDAYYFYpFLAAFGGYLFGKDGddpKDVGLNSPGAVAALEYLKDLIKDGVLPADaDYDAADALF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 248 KANRLASAMFGAWYEGTIRTNAADqsgKWGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMeNALATTNGQVT 327
Cdd:COG2182   252 AEGKAAMIINGPWAAADLKKALGI---DYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 328 MLRSQGLVPSLLTASKDAYVnqkqpywGNQTVWKTILDTLGD---VPA-ARGTQYFQDARQVMivvqADYIKGKyKTAQD 403
Cdd:COG2182   328 LFEATGRIPANKAAAEDAEV-------KADPLIAAFAEQAEYavpMPNiPEMGAVWTPLGTAL----QAIASGK-ADPAE 395

                         410
                  ....*....|..
gi 1751874397 404 ALNDAAKKISAA 415
Cdd:COG2182   396 ALDAAQKQIEAA 407
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 35-412 3.98e-29

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: 117.01  E-value: 3.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  35 KALESTIPSFNKKYPNVKVNVVDLGNQ-NVYdRGLAGCAAGGADM-PDVYSIEnneaeVFW-ARFPDCF--TDLNTLGAN 109
Cdd:cd14750    14 ELLKKAIAAFEKKHPDIKVEIEELPASsDDQ-RQQLVTALAAGSSaPDVLGLD-----VIWiPEFAEAGwlLPLTEYLKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 110 KYAKSFPAFKWTELTVGNKRYAMPW--DSGpvVIFYRRDLYQQAGVNPTaiKTWDDFIAAGKKVNAKFGGKVkmGAIGNG 187
Cdd:cd14750    88 EEDDDFLPATVEANTYDGKLYALPWftDAG--LLYYRKDLLEKYGPEPP--KTWDELLEAAKKRKAGEPGIW--GYVFQG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 188 QDDE----WFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVV--MTSDWGGQIT--AFKANRlaSAMFGA 259
Cdd:cd14750   162 KQYEglvcNFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISpkGVLTYGEEEAraAFQAGK--AAFMRN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 260 WYEGtIRTNAADQS---GKWGVYPMPASKaGGVRASNLGGSALALPSSSKNKAAAYAFMEnALATTNGQVTMLRSQGLVP 336
Cdd:cd14750   240 WPYA-YALLQGPESavaGKVGVAPLPAGP-GGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPP 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751874397 337 SLLTASKDAYVNQKQPYwgnqtvWKTILDTLgdvPAARG---TQYFQDARQVMIVVQADYIKGKyKTAQDALNDAAKKI 412
Cdd:cd14750   317 TRRALYDDPEVLEAYPF------LPALLEAL---ENAVPrpvTPKYPEVSTAIQIALSAALSGQ-ATPEEALKQAQEKL 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 24-406 1.41e-28

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: 115.55  E-value: 1.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSW---DAAAKALESTIPSFNKKYPNVKVNVVDLGNQNvyDRGLAGCAAGGADMPDVYSIEnneaevFWARFPD-- 98
Cdd:cd14749     1 TITYWQYftgDTKKKYMDELIADFEKENPNIKVKVVVFPYDN--YKTKLKTAVAAGEGPDVFNLW------PGGWLAEfv 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  99 ---CFTDLN-TLGANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNpTAIKTWDDFIAAGKKVNAK 174
Cdd:cd14749    73 kagLLLPLTdYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPKTWDELIEAAKKDKFK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 175 FGGKVKMGAIGNGQDDEWFR-MLANQN-GCFYFDNTASQITIAKSGCVQALDTVKKLFANDvVMTSDWGG-----QITAF 247
Cdd:cd14749   152 AKGQTGFGLLLGAQGGHWYFqYLVRQAgGGPLSDDGSGKATFNDPAFVQALQKLQDLVKAG-AFQEGFEGidyddAGQAF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 248 KANRLASAMFGAWYEGTIRTNAADqsGKWGVYPMPASKAGGVRASNLGGS-ALALPSSSKNKAAAYAFMeNALATTNGQV 326
Cdd:cd14749   231 AQGKAAMNIGGSWDLGAIKAGEPG--GKIGVFPFPTVGKGAQTSTIGGSDwAIAISANGKKKEAAVKFL-KYLTSPEVMK 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 327 TMLRSQGLVPSLLTASKDAYVNQKQPY-----WGNQTVWKTILDTlgdvPAARGTQYFQDARQVMIVVQADYiKGKYKTA 401
Cdd:cd14749   308 QYLEDVGLLPAKEVVAKDEDPDPVAILgpfadVLNAAGSTPFLDE----YWPAAAQVHKDAVQKLLTGKIDP-EQVVKQA 382


                  ....*
gi 1751874397 402 QDALN 406
Cdd:cd14749   383 QSAAA 387
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 24-412 5.49e-22

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: 96.68  E-value: 5.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVW--SWDAAAKALESTIPSFNKKYPNVKVNVV-----DLGNQnvydrglAGCAAGGADMPDVYsiennEAEVFW-AR 95
Cdd:cd14751     1 TITFWhtSSDEEKVLYEKLIPAFEKEYPKIKVKAVrvpfdGLHNQ-------IKTAAAGGQAPDVM-----RADIAWvPE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  96 FP--DCFTDLNTLGANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTaiKTWDDFIAAGKKVNA 173
Cdd:cd14751    69 FAklGYLQPLDGTPAFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKK 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 174 KFGgkvKMGAIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVV---MTSDWGGQITAFKAN 250
Cdd:cd14751   147 KKG---RYGLYISGDGPYWLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAItpcASGGYPNMQDGFKSG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 251 RLASAMFGAW-YEGTIRTNAADQSGKWGVYPMPASKAGgvRASNLGGSALALPSSSKNKAAAYAFMENALATTNgQVTML 329
Cdd:cd14751   224 RYAMIVNGPWaYADILGGKEFKDPDNLGIAPVPAGPGG--SGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEA-QALTA 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 330 RSQGLVPSLLTASKDAYVNQ---KQPYwgnqtvwKTILDT-LGDVPAARGTQYFQDARQVMivvqADYIKGKyKTAQDAL 405
Cdd:cd14751   301 AKLGLLPTRTSAYESPEVANnpmVAAF-------KPALETaVPRPPIPEWGELFEPLTLAF----AKVLRGE-KSPREAL 368


                  ....*..
gi 1751874397 406 NDAAKKI 412
Cdd:cd14751   369 DEAAKQW 375
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-347 1.13e-20

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: 92.74  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSW-DAAAKALESTIPSFNKKYpNVKVNVVDlgNQNVYDRGLAGCAAGGADMPDVYSIENNEAEVFWARfpDCFTD 102
Cdd:cd13586     1 TITVWTDeDGELEYLKELAEEFEKKY-GIKVEVVY--VDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAA--GLLAP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 103 LNTLGANKYAKSFPAFKwtELTVGNKRYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFIAAGKKVNAKFGGKVkmG 182
Cdd:cd13586    76 IPEYLAVKIKNLPVALA--AVTYNGKLYGVPVSVETIALFYNKDLV------PEPPKTWEELIALAKKFNDKAGGKY--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 183 AIGNGQDDEWFRMLANQNGCFYF---DNTASQITIAKSGCVQALDTVKKLFANDVVMTS--DWGGQITAFKANRLASAMF 257
Cdd:cd13586   146 FAYDQTNPYFSYPFLAAFGGYVFgenGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPdlDYDIADALFKEGKAAMIIN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 258 GAWYEGTIRTNAADqsgkWGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMENaLATTNGQVTMLRSQGLVPS 337
Cdd:cd13586   226 GPWDLADYKDAGIN----FGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEY-LTSDEAQLLLFEKTGRIPA 300

                         330
                  ....*....|
gi 1751874397 338 LLTASKDAYV 347
Cdd:cd13586   301 LKDALNDAAV 310
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 32-319 1.03e-18

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: 85.93  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  32 AAAKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAGCAAGGADmPDVYSIENNEAEVFWARfpDCFTDLNTLGANKY 111
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGP-ADVFASDNDWIAELAKA--GLLLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 112 AKSFPafkwteltvgnKRYAMPWDSGPVVIFYRRDLYQQAGVNPtaIKTWDDFIAAGKKVNAKFGGKVKMGAIGNGQDDE 191
Cdd:pfam01547  82 VLGVP-----------KLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 192 WF-RMLANQNGCFYFD-------NTASQITIAKSGCVQALDTVKKLFANDVVMTSDWGGQITAFKANRLASAMFGAWYEG 263
Cdd:pfam01547 149 YFtLALLASLGGPLFDkdgggldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 264 TIRT---------NAADQSGKWGVYPMPASKAGGVrasnlGGSALALPSSSKNKAAAYAFMENAL 319
Cdd:pfam01547 229 AANKvklkvafaaPAPDPKGDVGYAPLPAGKGGKG-----GGYGLAIPKGSKNKEAAKKFLDFLT 288
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-352 4.70e-18

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: 85.16  E-value: 4.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVWSWDAAA--KALESTIPSFNKKYPNVKVNVVDLGNQNVydRGLAGCAAGGADMPDVYSIENNEAEVFWARfpDCFT 101
Cdd:cd13522     1 TITVWHQYDTGenQAVNELIAKFEKAYPGITVEVTYQDTEAR--RQFFSTAAAGGKGPDVVFGPSDSLGPFAAA--GLLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 DLNTLGANKYAKSFPAFKWTELtvGNKRYAMPWDSGPVVIFYRRDLyqqagVNPTAIKTWDDFIAAGKKVNAKfggkVKM 181
Cdd:cd13522    77 PLDEYVSKSGKYAPNTIAAMKL--NGKLYGVPVSVGAHLMYYNKKL-----VPKNPPKTWQELIALAQGLKAK----NVW 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 182 GAIGNGQDDEWFRMLANQNG--CFYFDNTASQITIAKSGCVQALDTVKKLFANDVVMTSDWGGQI--TAFKANRLASAMF 257
Cdd:cd13522   146 GLVYNQNEPYFFAAWIGGFGgqVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIadALFKAGKAAMIIN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 258 GAWYEGTIRTNAADqsgKWGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMENALATTNGQVtMLRSQGLVPS 337
Cdd:cd13522   226 GPWDLGDYRQALKI---NLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLV-LFDDAGDIPA 301

                         330
                  ....*....|....*
gi 1751874397 338 LLTASKDAYVNQKQP 352
Cdd:cd13522   302 NLQAYESPAVQNKPA 316
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 24-347 4.34e-12

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: 67.02  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  24 TVTVW-SWDAA-AKALESTIPSFNKKYPNVKVNVVDLGNQNVYDRGLAgcaaggadmpdvySIENNEAevfwarfPDCFT 101
Cdd:cd13657     1 TITIWhALTGAeEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLT-------------AIPAGEG-------PDLFI 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 102 ----------------DLNTLGANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFI 165
Cdd:cd13657    61 wahdwigqfaeagllvPISDYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALV------DQPPETTDELL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 166 AAGKKVNAKFGGKvkMGAIGNGQDDEWFRMLANQNGCFYFDNTASQITIAKSGCVQALDTVKKLFANDVVMTSDWGGQIT 245
Cdd:cd13657   135 AIMKDHTDPAAGS--YGLAYQVSDAYFVSAWIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQTS 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 246 AFKANRLASAMFGAWYEGTIRTNAADqsgkWGVYPMPASKAGGVRASNLG--GSALALPSSSKNKAAAYAFMEnALATTN 323
Cdd:cd13657   213 LFNEGKAAMIINGPWFIGGIKAAGID----LGVAPLPTVDGTNPPRPYSGveGIYVTKYAERKNKEAALDFAK-FFTTAE 287

                         330       340
                  ....*....|....*....|....
gi 1751874397 324 GQVTMLRSQGLVPSLLTASKDAYV 347
Cdd:cd13657   288 ASKILADENGYVPAATNAYDDAEV 311
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 98-347 5.70e-11

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 62.81  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  98 DCFTDLNTLganKYAKSFPAFKwTELTVGNKRYAMPWD-SGPVVIFYRRDLYQQAGVNPtaiKTWDDFIAAGKKVNAKFG 176
Cdd:pfam13416  57 GLLADLSDV---DNLDDLPDAL-DAAGYDGKLYGVPYAaSTPTVLYYNKDLLKKAGEDP---KTWDELLAAAAKLKGKTG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 177 gkvkMGAIGNGqddeWFRMLANQNGCFYFDNTASQITIaksgcVQALDTVKKlFANDVVMTSDWGGQITAFKANRLASAM 256
Cdd:pfam13416 130 ----LTDPATG----WLLWALLADGVDLTDDGKGVEAL-----DEALAYLKK-LKDNGKVYNTGADAVQLFANGEVAMTV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 257 FGAWyegtIRTNAADQSGKWG-VYPMPaskaggvrASNLGGSALALPSSSKNK-AAAYAFMeNALATTNGQVTMLRSQGL 334
Cdd:pfam13416 196 NGTW----AAAAAKKAGKKLGaVVPKD--------GSFLGGKGLVVPAGAKDPrLAALDFI-KFLTSPENQAALAEDTGY 262

                         250
                  ....*....|...
gi 1751874397 335 VPSLLTASKDAYV 347
Cdd:pfam13416 263 IPANKSAALSDEV 275
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 123-326 8.00e-09

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: 57.11  E-value: 8.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 123 LTVGNKRYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFIAAGKKVNAKFGGKVKM-----------GAIGnGQDDE 191
Cdd:cd13658    94 LTYDGKLYGLPAAVETLALYYNKDLV------KNAPKTFDELEALAKDLTKEKGKQYGFladatnfyysyGLLA-GNGGY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 192 WFRmlanQNGCFYFDNtasQITIAKSGCVQALDTVKKLFANDVV---MTSDWggQITAFKANRLASAMFGAWyegtiRTN 268
Cdd:cd13658   167 IFK----KNGSDLDIN---DIGLNSPGAVKAVKFLKKWYTEGYLpkgMTGDV--IQGLFKEGKAAAVIDGPW-----AIQ 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1751874397 269 AADQSGK-WGVYPMPASKAGGVRASNLGGSALALPSSSKNKAAAYAFMENALATTNGQV 326
Cdd:cd13658   233 EYQEAGVnYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKK 291
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
111-315 1.74e-08

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 55.69  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 111 YAKSFPAFKWTELTVGNKrYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFIaagkkvNAKFGGKVkmgAIGNGQDd 190
Cdd:COG0687   108 LANLDPRFKDPPFDPGNV-YGVPYTWGTTGIAYNTDKV------KEPPTSWADLW------DPEYKGKV---ALLDDPR- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 191 EWFRMLANQNGCFYFDNTASQITiaksgcvQALDTVKKLFANDVVMTSDWGGQITAFKANRLASAMfgaWYEGTIRTnAA 270
Cdd:COG0687   171 EVLGAALLYLGYDPNSTDPADLD-------AAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAV---GWSGDALA-LR 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1751874397 271 DQSGKWG-VYPmpasKAGgvraSNLGGSALALPSSSKNKAAAYAFM 315
Cdd:COG0687   240 AEGPPIAyVIP----KEG----ALLWFDNMAIPKGAPNPDLAYAFI 277
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
110-324 2.25e-05

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 46.16  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 110 KYAKSFPAFKWTELTVGNKRYAMPWDSGPVVIFYRRDLYqqagvnPTAIKTWDDFIAAGKKVNAKfgGKvkmGAIGNGQD 189
Cdd:PRK09474  110 AFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLV------PTPPKTWEEIPALDKELKAK--GK---SAIMWNLQ 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 190 DEWFR--MLANQNG-CFYFDN---TASQITIAKSGCVQALDTVKKLFANDVV-MTSDWGGQITAFKANRLASAMFGAWYE 262
Cdd:PRK09474  179 EPYFTwpLIAADGGyAFKFENggyDVKDVGVNNAGAKAGLQFLVDLVKNKHMnADTDYSIAEAAFNKGETAMTINGPWAW 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751874397 263 GTIrtnaaDQSG-KWGVYPMPASKAGGVRASnLGGSALALPSSSKNKAAAYAFMENALATTNG 324
Cdd:PRK09474  259 SNI-----DKSGiNYGVTVLPTFNGKPSKPF-VGVLSAGINAASPNKELAKEFLENYLLTDEG 315
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 111-341 8.58e-05

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: 44.21  E-value: 8.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 111 YAKSFPAFKWT-ELTVGNKRYAMPWDSGPVVIFYRRDLYQQAGVNPTA----------IKTWDDFIAAgkkvnakfggkV 179
Cdd:cd13588    79 YANIDPRLRNLpWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLAllwdpkykgrVAARDDPIDA-----------I 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 180 KMGAIGNGQDDEwfrmlanqngcfyFDNTASQITIAKSGCVQALDTVKK----------LFAN-DVVMTSDWGGQITAF- 247
Cdd:cd13588   148 ADAALYLGQDPP-------------FNLTDEQLDAVKAKLREQRPLVRKywsdgaelvqLFANgEVVAATAWSGQVNALq 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 248 KANRLASAMFGAwyEGTirTNAADqsgkwgvypmpaskaggvrasnlggsALALPSSSKNKAAAYAFMENAL-ATTNGQV 326
Cdd:cd13588   215 KAGKPVAYVIPK--EGA--TGWVD--------------------------TWMILKDAKNPDCAYKWLNYMLsPKVQAAV 264

                         250
                  ....*....|....*
gi 1751874397 327 TMlrSQGLVPSLLTA 341
Cdd:cd13588   265 AE--WTGYAPSNPEA 277
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 124-347 1.01e-03

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: 41.18  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 124 TVGNKRYAMPWDSGPVVIFYRRDLYQQAGVnptaiKTWDDFIAAGKKVNAKFGGKvkmgaIGNGqddeW-FRMLANQNGC 202
Cdd:cd13655    97 TYNGKLYGYPFTANTWFMYYDKSKLTEDDV-----KSLDTMLAKAPDAKGKVSFD-----LSNS----WyLYAFFFGAGC 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 203 FYFDNT---ASQITIAKSGCVQALDTVKKLFANDVVMTSDWGGQITAFKANRLASAMFGAWyegtirtNAADQSGKWG-- 277
Cdd:cd13655   163 KLFGNNggdTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGDAISGLKDGTLGAGVSGPW-------DAANLKKALGdn 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751874397 278 --VYPMPASKAGGVRA---SNLGGSALALPSSSKNKAAAYAFMEnALATTNGQVTMLRSQGLVPSLLTASKDAYV 347
Cdd:cd13655   236 yaVAKLPTYTLGGKDVqmkSFAGYKAIGVNSNTKNPEAAMALAD-YLTNEESQLTRFEKRGIGPTNKEAAESDAV 309
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 77-328 1.64e-03

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: 40.52  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397  77 DMPDVYSIENNEAEVFWARFPDCFTDLNTL-----GANKYAKSFPAFKWTELTVGNKRYAMPWDSGPVV----IFYRRDL 147
Cdd:cd13521    56 DLPDIVGADYLKDKFIAYGMEGAFLPLSKYidqypNLKAFFKQHPDVLRASTASDGKIYLIPYEPPKDVpnqgYFIRKDW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 148 YQQAGVNPtaIKTWDDFIAAGKKVNAK----FGGKVKMGAIGNGQDDEWFRMLA---------NQNGCFYFDNTASQITI 214
Cdd:cd13521   136 LDKLNLKT--PKTLDELYNVLKAFKEKdpngNGKADEIPFIDRDPLYGAFRLINswgarsaggSTDSDWYEDNGKFKHPF 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751874397 215 AKSGCVQALDTVKKLFaNDVVMTSDWGGQITAFKANRLAS----AMFGAWYEGTIRTNAADQSGK--WGVYPMPASKAGG 288
Cdd:cd13521   214 ASEEYKDGMKYMNKLY-TEGLIDKESFTQKDDQAEQKFSNgklgGFTHNWFASDNLFTAQLGKEKpmYILLPIAPAGNVK 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1751874397 289 VR-----ASNLGGSALALPSSSKNKAAAYAFMeNALATTNGQVTM 328
Cdd:cd13521   293 GRreedsPGYTGPDGVAISKKAKNPVAALKFF-DWLASEEGRELA 336
 
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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