|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
6-388 |
2.82e-25 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 106.28 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 6 IFGALAISGILIFALFVGQGTSNTVGS----ITVWGT--LDQGAFSTVIRQASENTGELSgVVYEQKDAATYDAELTNAL 79
Cdd:COG1653 4 LALALAAALALALAACGGGGSGAAAAAgkvtLTVWHTggGEAAALEALIKEFEAEHPGIK-VEVESVPYDDYRTKLLTAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 80 ANGQGPDIFLMREDQAMKNVGKVYVIPY--AILSESEFEATFAVAATPFLTAGG-IEAIPLNVDPLVLYWNRDLLASAGR 156
Cdd:COG1653 83 AAGNAPDVVQVDSGWLAEFAAAGALVPLddLLDDDGLDKDDFLPGALDAGTYDGkLYGVPFNTDTLGLYYNKDLFEKAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 157 TlPPQYWDEVIpmatyvvdgskelnASAVTLRDQAGTIkksAIAFGeyqniSDAKDILAALILQAGGLITTKDSaghivs 236
Cdd:COG1653 163 D-PPKTWDELL--------------AAAKKLKAKDGVY---GFALG-----GKDGAAWLDLLLSAGGDLYDEDG------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 237 slsqKATKGAQATVNALRFYT-----GFADPSRDIYSWNrslpDARAAFAAGDVGLYVGHASEESLIRQMNPNLNFFVAA 311
Cdd:COG1653 214 ----KPAFDSPEAVEALEFLKdlvkdGYVPPGALGTDWD----DARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAP 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818893430 312 LPQIRGSDYSEGTAHVYGFAISRTSRNPTGAQTAAYLLASPELSKnlsialgipsaQISVLQAALQNTKT--KAYENLQ 388
Cdd:COG1653 286 LPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQA-----------KWDALQAVLLGQKTpeEALDAAQ 353
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
61-444 |
2.56e-22 |
|
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: 98.13 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYE-QKDAATYDAELTNALANGQGPDIFLMREDQA--MKNVGKVYVIPYAILSESEFEATFAvaaTPFLTAGGIE---- 133
Cdd:cd14748 32 VKAVyQGSYDDTLTKLLAALAAGTAPDVAQVDASWVaqLADSGALEPLDDYIDKDGVDDDDFY---PAALDAGTYDgkly 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 134 AIPLNVDPLVLYWNRDLLASAGRTL--PPQYWDEVIpmatyvvdgskelnASAVTLRDQAGTIKKSAIAFGEYQNISdak 211
Cdd:cd14748 109 GLPFDTSTPVLYYNKDLFEEAGLDPekPPKTWDELE--------------EAAKKLKDKGGKTGRYGFALPPGDGGW--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 212 dILAALILQAGglittkdsaGHIVSSLSQKATKGAQATVNALRFYTGFADPSRdiYSWNRSLPDARAAFAAGDVGLYVGH 291
Cdd:cd14748 172 -TFQALLWQNG---------GDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDG--VSPLNDWGDAQDAFISGKVAMTING 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 292 ASEESLIRQMNPNLNFFVAALPQIRGsdySEGTAHVYGFAISrTSRNPTGAQTAAY----LLASPELSKNLSIALGIPSA 367
Cdd:cd14748 240 TWSLAGIRDKGAGFEYGVAPLPAGKG---KKGATPAGGASLV-IPKGSSKKKEAAWefikFLTSPENQAKWAKATGYLPV 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818893430 368 QISVLQAALQNTKtkayENLQIKASHDQaiaLSAITARAWVDPDPQETDTIFRAMIENTVSGALRIEDAIQRADQEL 444
Cdd:cd14748 316 RKSAAEDPEEFLA----ENPNYKVAVDQ---LDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
61-353 |
4.79e-11 |
|
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: 63.59 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYEQKDAATYDAELTNALANGQGP-DIFLMREDQAMKNVGKVYVIPYailsesefeaTFAVAATPFLTAGGIEAIPLNV 139
Cdd:pfam01547 26 VEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPL----------DDYVANYLVLGVPKLYGVPLAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 140 DPLVLYWNRDLLASAGRTlPPQYWDEVIPMAtyvvdgsKELNASavtlrdqagtiKKSAIAFGEYQNISDAKDILAALIL 219
Cdd:pfam01547 96 ETLGLIYNKDLFKKAGLD-PPKTWDELLEAA-------KKLKEK-----------GKSPGGAGGGDASGTLGYFTLALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 220 QAGGLITTKDSAGhivssLSQKATKGAQATVNALRFYTGFADPSRDIYSWNRSLPDARAAFAAGDVGLYVGHASEESLIR 299
Cdd:pfam01547 157 SLGGPLFDKDGGG-----LDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 300 QMNPNLNFFVAALPQIRGSDY------SEGTAHVYGFAISRTSRNPTGAQTAAYLLASPE 353
Cdd:pfam01547 232 KVKLKVAFAAPAPDPKGDVGYaplpagKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-338 |
7.94e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 47.70 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 1 MILLVIFGALAISGILIFALFVGQGTSNTVGSITVWGTLDQG--AFSTVIRQASENTGelSGVVYEQKDAATydAELTNA 78
Cdd:PRK09474 1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGynGLAEVGKKFEKDTG--IKVTVEHPDKLE--EKFPQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 79 LANGQGPDIFLMREDQAmknvGkvyviPYA---ILSESEFEATFAVAATPF----LTAGG-IEAIPLNVDPLVLYWNRDL 150
Cdd:PRK09474 77 AATGDGPDIIFWAHDRF----G-----GYAqsgLLAEVTPSKAFKDKLVPFtwdaVRYNGkLIGYPIAVEALSLIYNKDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 151 LASagrtlPPQYWDEVIPMatyvvdgSKELNASavtlrdqagtiKKSAIAFgEYQNISDAKDILAAlilqAGGLITTKDS 230
Cdd:PRK09474 148 VPT-----PPKTWEEIPAL-------DKELKAK-----------GKSAIMW-NLQEPYFTWPLIAA----DGGYAFKFEN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 231 AGHIVSSLSQkATKGAQAtvnALRFYTGFADP---SRDI-YSwnrslpDARAAFAAGDVGLYVGHASEESLIRQmnPNLN 306
Cdd:PRK09474 200 GGYDVKDVGV-NNAGAKA---GLQFLVDLVKNkhmNADTdYS------IAEAAFNKGETAMTINGPWAWSNIDK--SGIN 267
|
330 340 350
....*....|....*....|....*....|..
gi 818893430 307 FFVAALPQIRGSDySEGTAHVYGFAISRTSRN 338
Cdd:PRK09474 268 YGVTVLPTFNGKP-SKPFVGVLSAGINAASPN 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
6-388 |
2.82e-25 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 106.28 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 6 IFGALAISGILIFALFVGQGTSNTVGS----ITVWGT--LDQGAFSTVIRQASENTGELSgVVYEQKDAATYDAELTNAL 79
Cdd:COG1653 4 LALALAAALALALAACGGGGSGAAAAAgkvtLTVWHTggGEAAALEALIKEFEAEHPGIK-VEVESVPYDDYRTKLLTAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 80 ANGQGPDIFLMREDQAMKNVGKVYVIPY--AILSESEFEATFAVAATPFLTAGG-IEAIPLNVDPLVLYWNRDLLASAGR 156
Cdd:COG1653 83 AAGNAPDVVQVDSGWLAEFAAAGALVPLddLLDDDGLDKDDFLPGALDAGTYDGkLYGVPFNTDTLGLYYNKDLFEKAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 157 TlPPQYWDEVIpmatyvvdgskelnASAVTLRDQAGTIkksAIAFGeyqniSDAKDILAALILQAGGLITTKDSaghivs 236
Cdd:COG1653 163 D-PPKTWDELL--------------AAAKKLKAKDGVY---GFALG-----GKDGAAWLDLLLSAGGDLYDEDG------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 237 slsqKATKGAQATVNALRFYT-----GFADPSRDIYSWNrslpDARAAFAAGDVGLYVGHASEESLIRQMNPNLNFFVAA 311
Cdd:COG1653 214 ----KPAFDSPEAVEALEFLKdlvkdGYVPPGALGTDWD----DARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAP 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818893430 312 LPQIRGSDYSEGTAHVYGFAISRTSRNPTGAQTAAYLLASPELSKnlsialgipsaQISVLQAALQNTKT--KAYENLQ 388
Cdd:COG1653 286 LPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQA-----------KWDALQAVLLGQKTpeEALDAAQ 353
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
61-444 |
2.56e-22 |
|
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: 98.13 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYE-QKDAATYDAELTNALANGQGPDIFLMREDQA--MKNVGKVYVIPYAILSESEFEATFAvaaTPFLTAGGIE---- 133
Cdd:cd14748 32 VKAVyQGSYDDTLTKLLAALAAGTAPDVAQVDASWVaqLADSGALEPLDDYIDKDGVDDDDFY---PAALDAGTYDgkly 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 134 AIPLNVDPLVLYWNRDLLASAGRTL--PPQYWDEVIpmatyvvdgskelnASAVTLRDQAGTIKKSAIAFGEYQNISdak 211
Cdd:cd14748 109 GLPFDTSTPVLYYNKDLFEEAGLDPekPPKTWDELE--------------EAAKKLKDKGGKTGRYGFALPPGDGGW--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 212 dILAALILQAGglittkdsaGHIVSSLSQKATKGAQATVNALRFYTGFADPSRdiYSWNRSLPDARAAFAAGDVGLYVGH 291
Cdd:cd14748 172 -TFQALLWQNG---------GDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDG--VSPLNDWGDAQDAFISGKVAMTING 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 292 ASEESLIRQMNPNLNFFVAALPQIRGsdySEGTAHVYGFAISrTSRNPTGAQTAAY----LLASPELSKNLSIALGIPSA 367
Cdd:cd14748 240 TWSLAGIRDKGAGFEYGVAPLPAGKG---KKGATPAGGASLV-IPKGSSKKKEAAWefikFLTSPENQAKWAKATGYLPV 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818893430 368 QISVLQAALQNTKtkayENLQIKASHDQaiaLSAITARAWVDPDPQETDTIFRAMIENTVSGALRIEDAIQRADQEL 444
Cdd:cd14748 316 RKSAAEDPEEFLA----ENPNYKVAVDQ---LDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
32-367 |
6.87e-21 |
|
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: 93.98 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 32 SITVW----GTLDQGAFSTVIRQ-ASENTG-ELSGVVYEQKDAATydaELTNALANGQGPDIFLMR---EDQAMKNVGKV 102
Cdd:cd14749 1 TITYWqyftGDTKKKYMDELIADfEKENPNiKVKVVVFPYDNYKT---KLKTAVAAGEGPDVFNLWpggWLAEFVKAGLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 103 YVIPYAILSESEFEATFAVAATPFLTAGGIEAIPLNVDPLVLYWNRDLLASAGRTLPPQYWDEVIPMATYVVDGSKELNA 182
Cdd:cd14749 78 LPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 183 SAVTLRDQAGtikksaiaFGEYQNisdakdilaaLILQAGGLITTKDsaghivssLSQKATKGAQATVNALRFYT----- 257
Cdd:cd14749 158 FGLLLGAQGG--------HWYFQY----------LVRQAGGGPLSDD--------GSGKATFNDPAFVQALQKLQdlvka 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 258 ---GFADPSRDIyswnrslPDARAAFAAGDVGLYVGHASEESLIRQMNPNLNFFVAALPQIRGSD-YSEGTAHVYGFAIS 333
Cdd:cd14749 212 gafQEGFEGIDY-------DDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGKGAqTSTIGGSDWAIAIS 284
|
330 340 350
....*....|....*....|....*....|....
gi 818893430 334 RTSRNPTGAQTAAYLLASPELSKNLSIALGIPSA 367
Cdd:cd14749 285 ANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPA 318
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
33-444 |
1.53e-19 |
|
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: 89.77 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 33 ITVWgTLDQGAFSTVIRQA-----SENTG-ElsgVVYEQKDAATYDAELTNALANGQGPDIFLMREdqamknvgkVYVIP 106
Cdd:cd13585 2 LTFW-DWGQPAETAALKKLidafeKENPGvK---VEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDG---------PWVPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 107 YA----------ILSESEFEATFAVAATPFLTAGG-IEAIPLNVDPLVLYWNRDLLASAGRTL-PPQYWDEvipmatyVV 174
Cdd:cd13585 69 FAsngalldlddYIEKDGLDDDFPPGLLDAGTYDGkLYGLPFDADTLVLFYNKDLFDKAGPGPkPPWTWDE-------LL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 175 DGSKELNasavtlrdqAGTIKKSAIAFGEYQNISdakDILAALILQAGGLITTKDsaghivsslSQKATKGAQATVNALR 254
Cdd:cd13585 142 EAAKKLT---------DKKGGQYGFALRGGSGGQ---TQWYPFLWSNGGDLLDED---------DGKATLNSPEAVEALQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 255 FYTGFAD----PSRDIYSWNrslpDARAAFAAGDVGLYVGHASEESLIRQMNPNLNFFVAALPQIRGSDYSeGTAHVYGF 330
Cdd:cd13585 201 FYVDLYKdgvaPSSATTGGD----EAVDLFASGKVAMMIDGPWALGTLKDSKVKFKWGVAPLPAGPGGKRA-SVLGGWGL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 331 AISRTSRNPTGAQTAAYLLASPELSKNLSIALGIPSAQISVLQAALQNTKTKAYENLQIKASHDQAIALSAITARAWVDP 410
Cdd:cd13585 276 AISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPI 355
|
410 420 430
....*....|....*....|....*....|....
gi 818893430 411 DPQETDTIFRAMIENTVsgalriEDAIQRADQEL 444
Cdd:cd13585 356 LSEALQEALLGALGKSP------EEALKEAAKEI 383
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
6-444 |
2.38e-18 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 86.54 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 6 IFGALAISGILIFAL-FVGQGTSNTV--------GSITVWGTLDQG-AFSTVIRQASENTGElsGVVYEQKDAATYDAEL 75
Cdd:COG2182 5 LLAALALALALALALaACGSGSSSSGsssaagagGTLTVWVDDDEAeALEEAAAAFEEEPGI--KVKVVEVPWDDLREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 76 TNALANGQGPDIFLMREDQAMKNV--GKVYVIPYAILSESEFEATFAVAATpflTAGGIEAIPLNVDPLVLYWNRDLLAS 153
Cdd:COG2182 83 TTAAPAGKGPDVFVGAHDWLGELAeaGLLAPLDDDLADKDDFLPAALDAVT---YDGKLYGVPYAVETLALYYNKDLVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 154 AgrtlPPQYWDEVIPMAtyvvdgsKELNASAvtlrdqagtikKSAIAFgeyqnisDAKDI--LAALILQAGGLITTKDSA 231
Cdd:COG2182 160 E----PPKTWDELIAAA-------KKLTAAG-----------KYGLAY-------DAGDAyyFYPFLAAFGGYLFGKDGD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 232 GhivsslSQKATKGAQATVNALRFYTGFADpsRDIYSWNRSLPDARAAFAAGDVGLYVGHASEESLIRQmNPNLNFFVAA 311
Cdd:COG2182 211 D------PKDVGLNSPGAVAALEYLKDLIK--DGVLPADADYDAADALFAEGKAAMIINGPWAAADLKK-ALGIDYGVAP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 312 LPQIRGSDYSEGTAHVYGFAISRTSRNPTGAQTAAYLLASPELSKNLSIALGipsaQISVLQAALQNTKTKAYENLQ-IK 390
Cdd:COG2182 282 LPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATG----RIPANKAAAEDAEVKADPLIAaFA 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 818893430 391 ASHDQAIALSAITARAWVdpdpqetDTIFRAMIENTVSGALRIEDAIQRADQEL 444
Cdd:COG2182 358 EQAEYAVPMPNIPEMGAV-------WTPLGTALQAIASGKADPAEALDAAQKQI 404
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
61-444 |
6.56e-15 |
|
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: 76.18 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYEQKDAATYDAELTNALANG-QGPDIFLMreDqamknvgkVYVIP-----------YAILSESEFEATF-AVAATPfl 127
Cdd:cd14750 34 IEELPASSDDQRQQLVTALAAGsSAPDVLGL--D--------VIWIPefaeagwllplTEYLKEEEDDDFLpATVEAN-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 128 TAGG-IEAIPLNVDPLVLYWNRDLLASAGRTlPPQYWDEVIPMATYVVDGSKELNASAVTLRDQAGTIkksaiafgeyqn 206
Cdd:cd14750 102 TYDGkLYALPWFTDAGLLYYRKDLLEKYGPE-PPKTWDELLEAAKKRKAGEPGIWGYVFQGKQYEGLV------------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 207 iSDAKDILAAlilqAGGlittkdsagHIVSSLSQKATKGAQATVNALRFYTGFAD---PSRDIYSWNRslPDARAAFAAG 283
Cdd:cd14750 169 -CNFLELLWS----NGG---------DIFDDDSGKVTVDSPEALEALQFLRDLIGegiSPKGVLTYGE--EEARAAFQAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 284 DVGL-------YVGHASEESLIRQmnpnlNFFVAALPQIRGSDySEGTAHVYGFAISRTSRNPTGAQTAAYLLASPELSK 356
Cdd:cd14750 233 KAAFmrnwpyaYALLQGPESAVAG-----KVGVAPLPAGPGGG-SASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 357 NLSIALGIPSAQISVlqaalqntktkaYENLQIKAS--HDQAI--ALSAITARAwVDPDPQETDTIFRAMIENTVSGALR 432
Cdd:cd14750 307 RRAINGGLPPTRRAL------------YDDPEVLEAypFLPALleALENAVPRP-VTPKYPEVSTAIQIALSAALSGQAT 373
|
410
....*....|..
gi 818893430 433 IEDAIQRADQEL 444
Cdd:cd14750 374 PEEALKQAQEKL 385
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
32-444 |
1.44e-13 |
|
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: 71.96 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 32 SITVW---GTLDQGAFSTVIRQ-ASENTGelSGVVYEQKDAATYDAELTNALANGQGPDIFLMREDQAMK--NVGKVYVI 105
Cdd:cd14747 1 TLTVWamgNSAEAELLKELADEfEKENPG--IEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEfaAMGALEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 106 PYAILSESEFEATFAVAATPFLTAGGIEAIPLNVDPLVLYWNRDLLASAGRTLPPQYWDEVIpmatyvvdgskelnasAV 185
Cdd:cd14747 79 TPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELE----------------AA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 186 TLRDQAGTIKKSAIAFG----EYQNisdakdiLAALILQAGGLITTKDSAghiVSSLSQkatkgaQATVNALRFYTGF-- 259
Cdd:cd14747 143 AKKIKADGPDVSGFAIPgkndVWHN-------ALPFVWGAGGDLATKDKW---KATLDS------PEAVAGLEFYTSLyq 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 260 ---ADPSRDIYSwnrslPDARAAFAAGDVGLYVGHASEESLIRQMNPNL--NFFVAALPqirGSDYSEGTAHVYG--FAI 332
Cdd:cd14747 207 kglSPKSTLENS-----ADVEQAFANGKVAMIISGPWEIGAIREAGPDLagKWGVAPLP---GGPGGGSPSFAGGsnLAV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 333 SRTSRNPTGAQTAAYLLASPElsknlsialgipsAQISVLQAA--LQNTkTKAYENLQIKASH-DQAIALSAITARAwVD 409
Cdd:cd14747 279 FKGSKNKDLAWKFIEFLSSPE-------------NQAAYAKATgmLPAN-TSAWDDPSLANDPlLAVFAEQLKTGKA-TP 343
|
410 420 430
....*....|....*....|....*....|....*...
gi 818893430 410 PDPQ--ETDTIFRAMIENTVSG-ALRIEDAIQRADQEL 444
Cdd:cd14747 344 ATPEwgEIEAELVLVLEEVWIGvGADVEDALDKAAAEI 381
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
33-378 |
6.89e-13 |
|
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: 69.75 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 33 ITVW---GTLDQGAFSTVIRQ-ASENTGELSGVVYEQKDAATYDaeLTNALANGQGPDIFLMREDQAMKNVGKVYVIPYA 108
Cdd:cd13522 2 ITVWhqyDTGENQAVNELIAKfEKAYPGITVEVTYQDTEARRQF--FSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 109 -ILSESEFEATFAVAATPFltAGGIEAIPLNVDPLVLYWNRDLLAsagrTLPPQYWDEVIPMATyvvdgskelnasavtl 187
Cdd:cd13522 80 eYVSKSGKYAPNTIAAMKL--NGKLYGVPVSVGAHLMYYNKKLVP----KNPPKTWQELIALAQ---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 188 rdQAGTIKKSAIAFGeYQNISDakdiLAALILQAGGLItTKDSAGHIVSSLSQKATKGAQATVNALRFYTGFADPSRDiY 267
Cdd:cd13522 138 --GLKAKNVWGLVYN-QNEPYF----FAAWIGGFGGQV-FKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETD-Y 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 268 SwnrslpDARAAFAAGDVGLYVGHASEESLIRQmNPNLNFFVAALPQIRGSDYSEGTAHVYGFAISRTSRNPTGAQTAAY 347
Cdd:cd13522 209 S------IADALFKAGKAAMIINGPWDLGDYRQ-ALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVK 281
|
330 340 350
....*....|....*....|....*....|..
gi 818893430 348 LLASPELSKNLSIALGIPSAQISVLQ-AALQN 378
Cdd:cd13522 282 YLTSYQAQLVLFDDAGDIPANLQAYEsPAVQN 313
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
61-353 |
4.79e-11 |
|
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: 63.59 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYEQKDAATYDAELTNALANGQGP-DIFLMREDQAMKNVGKVYVIPYailsesefeaTFAVAATPFLTAGGIEAIPLNV 139
Cdd:pfam01547 26 VEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPL----------DDYVANYLVLGVPKLYGVPLAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 140 DPLVLYWNRDLLASAGRTlPPQYWDEVIPMAtyvvdgsKELNASavtlrdqagtiKKSAIAFGEYQNISDAKDILAALIL 219
Cdd:pfam01547 96 ETLGLIYNKDLFKKAGLD-PPKTWDELLEAA-------KKLKEK-----------GKSPGGAGGGDASGTLGYFTLALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 220 QAGGLITTKDSAGhivssLSQKATKGAQATVNALRFYTGFADPSRDIYSWNRSLPDARAAFAAGDVGLYVGHASEESLIR 299
Cdd:pfam01547 157 SLGGPLFDKDGGG-----LDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 300 QMNPNLNFFVAALPQIRGSDY------SEGTAHVYGFAISRTSRNPTGAQTAAYLLASPE 353
Cdd:pfam01547 232 KVKLKVAFAAPAPDPKGDVGYaplpagKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
33-378 |
1.10e-10 |
|
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: 63.08 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 33 ITVWgtLDQGAFSTVIRQASENTGELSG--VVYEQKDAATYDAELTNALANGQGPDIFLMREDQAMKNV--GKVYVIPYA 108
Cdd:cd13586 2 ITVW--TDEDGELEYLKELAEEFEKKYGikVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAaaGLLAPIPEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 109 iLSESEFEATFAVAATPFltAGGIEAIPLNVDPLVLYWNRDLLASagrtlPPQYWDEVIpmatyvvdgskelnasAVTLR 188
Cdd:cd13586 80 -LAVKIKNLPVALAAVTY--NGKLYGVPVSVETIALFYNKDLVPE-----PPKTWEELI----------------ALAKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 189 DQAGTIKKSAIAFgeyqNISDAKDIlAALILQAGGLITTKDSAGHIVSSLSQKATKGAQATVNALRFYTGFADPSRDiys 268
Cdd:cd13586 136 FNDKAGGKYGFAY----DQTNPYFS-YPFLAAFGGYVFGENGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLD--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 269 wnrslPD-ARAAFAAGDVGLYVGHASEESLIRQMNpnLNFFVAALPQIRGSDYSEGTAHVYGFAISRTSRNPTGAQT-AA 346
Cdd:cd13586 208 -----YDiADALFKEGKAAMIINGPWDLADYKDAG--INFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEfAE 280
|
330 340 350
....*....|....*....|....*....|..
gi 818893430 347 YLLASPELSKNLSIALGIPSAQISVLQAALQN 378
Cdd:cd13586 281 YLTSDEAQLLLFEKTGRIPALKDALNDAAVKN 312
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
75-440 |
5.65e-08 |
|
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: 54.69 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 75 LTNALAnGQGPDIflMREDQA----MKNVGkvYVIPyaiLSESE-FEATFAVAATPFLTA---GGIEAIPLNVDPLVLYW 146
Cdd:cd14751 47 KTAAAG-GQAPDV--MRADIAwvpeFAKLG--YLQP---LDGTPaFDDIVDYLPGPMETNrynGHYYGVPQVTNTLALFY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 147 NRDLLASAGrTLPPQYWDEVIPMAtyvvdgskelnASAVTLRDQAGTikksaiafgeyqNIS-DAKDILAALILQAGGLI 225
Cdd:cd14751 119 NKRLLEEAG-TEVPKTMDELVAAA-----------KAIKKKKGRYGL------------YISgDGPYWLLPFLWSFGGDL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 226 TTKDSAGHIVSSlsqkatkgaQATVNALRFYTGFADpSRDIYSWNR-SLPDARAAFAAGDVGLYVG---HASEESLIRQM 301
Cdd:cd14751 175 TDEKKATGYLNS---------PESVRALETIVDLYD-EGAITPCASgGYPNMQDGFKSGRYAMIVNgpwAYADILGGKEF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 302 NPNLNFFVAALPQIRGsdyseGTAHVYG---FAISRTSRNPTGAQTAAYLLASPELSKNLSIALG-IPsaqisvlqaalq 377
Cdd:cd14751 245 KDPDNLGIAPVPAGPG-----GSGSPVGgedLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGlLP------------ 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818893430 378 nTKTKAYENLQIKASHDQAIALSAI---TARAWVdPDPQETDTIFRAMIENTVSGALRIEDAIQRA 440
Cdd:cd14751 308 -TRTSAYESPEVANNPMVAAFKPALetaVPRPPI-PEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
31-366 |
1.57e-07 |
|
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 52.98 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 31 GSITVWGTLDQG--AFSTVIRQASENTGelSGVVYEQKDAATydAELTNALANGQGPDIFLMREDQAMKNVGKvyvipyA 108
Cdd:cd13656 1 GKLVIWINGDKGynGLAEVGKKFEKDTG--IKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQS------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 109 ILSESEFEATFAVAATPF----LTAGG-IEAIPLNVDPLVLYWNRDLLasagrTLPPQYWDEVIPMatyvvdgSKELNAS 183
Cdd:cd13656 71 LLAEITPDKAFQDKLYPFtwdaVRYNGkLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPAL-------DKELKAK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 184 AvtlrdqagtikKSAIAFgEYQNISDAKDILAAlilqAGGLITTKDSAGHIVSSL---SQKATKGAQATVNALRFYTGFA 260
Cdd:cd13656 139 G-----------KSALMF-NLQEPYFTWPLIAA----DGGYAFKYENGKYDIKDVgvdNAGAKAGLTFLVDLIKNKHMNA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 261 DPSRDIyswnrslpdARAAFAAGDVGLYVGHASEESLIRQmnPNLNFFVAALPQIRGSDySEGTAHVYGFAISRTSRNPT 340
Cdd:cd13656 203 DTDYSI---------AEAAFNKGETAMTINGPWAWSNIDT--SKVNYGVTVLPTFKGQP-SKPFVGVLSAGINAASPNKE 270
|
330 340
....*....|....*....|....*....
gi 818893430 341 GAQT--AAYLLASPELSK-NLSIALGIPS 366
Cdd:cd13656 271 LAKEflENYLLTDEGLEAvNKDKPLGAVA 299
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
61-375 |
9.07e-07 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 50.10 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 61 VVYEQKDAATYDAELTNALANGQGPDI--FLMREDQAMKNVGKVYVIPyaiLSESEFEATFAVAATPFLTAGGIEAIPLN 138
Cdd:pfam13416 14 VEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLAD---LSDVDNLDDLPDALDAAGYDGKLYGVPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 139 VD-PLVLYWNRDLLASAGrtLPPQYWDEVipmatyvVDGSKELNASAVTLRDQAGTikksaiafgeyqnisdakdilAAL 217
Cdd:pfam13416 91 AStPTVLYYNKDLLKKAG--EDPKTWDEL-------LAAAAKLKGKTGLTDPATGW---------------------LLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 218 ILQAGGLITTKDsaghivsslsqkaTKGAQATVNALRFYTGFADpsrDIYSWNrSLPDARAAFAAGDVGLYVGHASEESL 297
Cdd:pfam13416 141 ALLADGVDLTDD-------------GKGVEALDEALAYLKKLKD---NGKVYN-TGADAVQLFANGEVAMTVNGTWAAAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 298 IRQMNPNlnfFVAALPQirgsdysEGT-AHVYGFAISRTSRNP-TGAQTAAYLLASPELSKNLSIALGIPSAQISVLQAA 375
Cdd:pfam13416 204 AKKAGKK---LGAVVPK-------DGSfLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSD 273
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
32-177 |
1.18e-06 |
|
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: 50.45 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 32 SITVWGTLDQG---AFSTVIRQ-ASENTGELSGVVYEQKdaATYDAELTNALANGQGPDIFLMREDQAMKNVGKVYVIPY 107
Cdd:cd13657 1 TITIWHALTGAeedALQQIIDEfEAKYPVPNVKVPFEKK--PDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818893430 108 AILSESEFEATFAVAATPFLT-AGGIEAIPLNVDPLVLYWNRDLLASagrtlPPQYWDEVIPMA---TYVVDGS 177
Cdd:cd13657 79 SDYLSEDDFENYLPTAVEAVTyKGKVYGLPEAYETVALIYNKALVDQ-----PPETTDELLAIMkdhTDPAAGS 147
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-338 |
7.94e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 47.70 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 1 MILLVIFGALAISGILIFALFVGQGTSNTVGSITVWGTLDQG--AFSTVIRQASENTGelSGVVYEQKDAATydAELTNA 78
Cdd:PRK09474 1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGynGLAEVGKKFEKDTG--IKVTVEHPDKLE--EKFPQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 79 LANGQGPDIFLMREDQAmknvGkvyviPYA---ILSESEFEATFAVAATPF----LTAGG-IEAIPLNVDPLVLYWNRDL 150
Cdd:PRK09474 77 AATGDGPDIIFWAHDRF----G-----GYAqsgLLAEVTPSKAFKDKLVPFtwdaVRYNGkLIGYPIAVEALSLIYNKDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 151 LASagrtlPPQYWDEVIPMatyvvdgSKELNASavtlrdqagtiKKSAIAFgEYQNISDAKDILAAlilqAGGLITTKDS 230
Cdd:PRK09474 148 VPT-----PPKTWEEIPAL-------DKELKAK-----------GKSAIMW-NLQEPYFTWPLIAA----DGGYAFKFEN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818893430 231 AGHIVSSLSQkATKGAQAtvnALRFYTGFADP---SRDI-YSwnrslpDARAAFAAGDVGLYVGHASEESLIRQmnPNLN 306
Cdd:PRK09474 200 GGYDVKDVGV-NNAGAKA---GLQFLVDLVKNkhmNADTdYS------IAEAAFNKGETAMTINGPWAWSNIDK--SGIN 267
|
330 340 350
....*....|....*....|....*....|..
gi 818893430 307 FFVAALPQIRGSDySEGTAHVYGFAISRTSRN 338
Cdd:PRK09474 268 YGVTVLPTFNGKP-SKPFVGVLSAGINAASPN 298
|
|
| |
