|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-344 |
2.65e-30 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 120.15 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 1 MNKFKPALASVMALAmivgLGACGSSNSSSDSssADGKITIKVQTFNnpgfgkPTSERPGADLWAKYEKAHPNVKIEETA 80
Cdd:COG1653 1 MRRLALALAAALALA----LAACGGGGSGAAA--AAGKVTLTVWHTG------GGEAAALEALIKEFEAEHPGIKVEVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 81 AASSDDARAaFNTAISTGsNAYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDWVAWK-----SESATVDGKLIGAGTDI 155
Cdd:COG1653 69 VPYDDYRTK-LLTALAAG-NAPDVVQVDSGWLAEFAAA-GALVPLDDLLDDDGLDKDDflpgaLDAGTYDGKLYGVPFNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 156 GPEGICYRADLLEKAGFPsdresvaewlggDDATWDSFFKAGKEYTEK---TGLPWYDSMASNWQSMINQVEESYVSKDD 232
Cdd:COG1653 146 DTLGLYYNKDLFEKAGLD------------PPKTWDELLAAAKKLKAKdgvYGFALGGKDGAAWLDLLLSAGGDLYDEDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 233 KIIAADNA------KIKDLYDQLTATKDMsahLTQWSDDWNAAFKSDTGFATIQCPaWLINNIKgNTGEDFQgWDIAdVF 306
Cdd:COG1653 214 KPAFDSPEavealeFLKDLVKDGYVPPGA---LGTDWDDARAAFASGKAAMMINGS-WALGALK-DAAPDFD-VGVA-PL 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2519265878 307 PGGGGNWGG------SYLVVPESSPVKDEAAKLVAWLTEADQQV 344
Cdd:COG1653 287 PGGPGGKKPasvlggSGLAIPKGSKNPEAAWKFLKFLTSPEAQA 330
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
40-432 |
9.27e-25 |
|
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: 104.79 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 40 TIKVQTFNNPGFGKPTserpgADLWAKYEKAHPNVKIEETAAASSDDARAaFNTAISTGsNAYDVYVAEVDWMPSLLAMp 119
Cdd:cd13585 1 TLTFWDWGQPAETAAL-----KKLIDAFEKENPGVKVEVVPVPYDDYWTK-LTTAAAAG-TAPDVFYVDGPWVPEFASN- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 120 DKFVDLSSY----TKDNDWVAWKSESATVDGKLIGAGTDIGPEGICYRADLLEKAGFPSDresvaewlggDDATWDSFFK 195
Cdd:cd13585 73 GALLDLDDYiekdGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK----------PPWTWDELLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 196 AGKEYTEKT------GLPWYDSMASNWQSMINQVEESYVSKDDKIIAADNAK-------IKDLYDQLTATKDmsahLTQW 262
Cdd:cd13585 143 AAKKLTDKKggqygfALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEavealqfYVDLYKDGVAPSS----ATTG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 263 SDDWNAAFKSDTgFATIQCPAWLINNIKgNTGEDFQgWDIAdVFPGGGGNWGGSY-----LVVPESSPVKDEAAKLVAWL 337
Cdd:cd13585 219 GDEAVDLFASGK-VAMMIDGPWALGTLK-DSKVKFK-WGVA-PLPAGPGGKRASVlggwgLAISKNSKHPEAAWKFIKFL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 338 TEADQQVSVFTTAnnyPSSEGAQASSDVSSKTDTYLNDAPTGKIFANRAKAYDIVPYKGSQYFDIQTKMVDALNRVdatQ 417
Cdd:cd13585 295 TSKENQLKLGGAA---GPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGA---L 368
|
410
....*....|....*
gi 2519265878 418 EQTPDQAWKQWLEDV 432
Cdd:cd13585 369 GKSPEEALKEAAKEI 383
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
62-367 |
3.11e-18 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 84.38 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 62 DLWAKYEKAHpNVKIEETAAASSDDARAaFNTAISTGSN-AYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDWVAWKsE 140
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQASNDLQAK-LLAAAAAGNApDLDVVWIAADQLATLAEA-GLLADLSDVDNLDDLPDAL-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 141 SATVDGKLIGAGTDIG-PEGICYRADLLEKAGfpsdresvaewlgGDDATWDSFFKAGKEYTEKTGlpWYDSmASNWQSM 219
Cdd:pfam13416 77 AAGYDGKLYGVPYAAStPTVLYYNKDLLKKAG-------------EDPKTWDELLAAAAKLKGKTG--LTDP-ATGWLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 220 INQVEESYVSKDDKiiaaDNAKIKDLYDQLTATKDMSAHlTQWSDDWNAAFKSDTgFATIQCPAWLINNIKGNtgedfqG 299
Cdd:pfam13416 141 ALLADGVDLTDDGK----GVEALDEALAYLKKLKDNGKV-YNTGADAVQLFANGE-VAMTVNGTWAAAAAKKA------G 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519265878 300 WDIADVFPGGGGNWGGSYLVVPESSPVKDEAA-KLVAWLTEADQQVSVFTTANNYPSSEGAQASSDVSS 367
Cdd:pfam13416 209 KKLGAVVPKDGSFLGGKGLVVPAGAKDPRLAAlDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKA 277
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-344 |
2.65e-30 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 120.15 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 1 MNKFKPALASVMALAmivgLGACGSSNSSSDSssADGKITIKVQTFNnpgfgkPTSERPGADLWAKYEKAHPNVKIEETA 80
Cdd:COG1653 1 MRRLALALAAALALA----LAACGGGGSGAAA--AAGKVTLTVWHTG------GGEAAALEALIKEFEAEHPGIKVEVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 81 AASSDDARAaFNTAISTGsNAYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDWVAWK-----SESATVDGKLIGAGTDI 155
Cdd:COG1653 69 VPYDDYRTK-LLTALAAG-NAPDVVQVDSGWLAEFAAA-GALVPLDDLLDDDGLDKDDflpgaLDAGTYDGKLYGVPFNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 156 GPEGICYRADLLEKAGFPsdresvaewlggDDATWDSFFKAGKEYTEK---TGLPWYDSMASNWQSMINQVEESYVSKDD 232
Cdd:COG1653 146 DTLGLYYNKDLFEKAGLD------------PPKTWDELLAAAKKLKAKdgvYGFALGGKDGAAWLDLLLSAGGDLYDEDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 233 KIIAADNA------KIKDLYDQLTATKDMsahLTQWSDDWNAAFKSDTGFATIQCPaWLINNIKgNTGEDFQgWDIAdVF 306
Cdd:COG1653 214 KPAFDSPEavealeFLKDLVKDGYVPPGA---LGTDWDDARAAFASGKAAMMINGS-WALGALK-DAAPDFD-VGVA-PL 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2519265878 307 PGGGGNWGG------SYLVVPESSPVKDEAAKLVAWLTEADQQV 344
Cdd:COG1653 287 PGGPGGKKPasvlggSGLAIPKGSKNPEAAWKFLKFLTSPEAQA 330
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
40-432 |
9.27e-25 |
|
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: 104.79 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 40 TIKVQTFNNPGFGKPTserpgADLWAKYEKAHPNVKIEETAAASSDDARAaFNTAISTGsNAYDVYVAEVDWMPSLLAMp 119
Cdd:cd13585 1 TLTFWDWGQPAETAAL-----KKLIDAFEKENPGVKVEVVPVPYDDYWTK-LTTAAAAG-TAPDVFYVDGPWVPEFASN- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 120 DKFVDLSSY----TKDNDWVAWKSESATVDGKLIGAGTDIGPEGICYRADLLEKAGFPSDresvaewlggDDATWDSFFK 195
Cdd:cd13585 73 GALLDLDDYiekdGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK----------PPWTWDELLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 196 AGKEYTEKT------GLPWYDSMASNWQSMINQVEESYVSKDDKIIAADNAK-------IKDLYDQLTATKDmsahLTQW 262
Cdd:cd13585 143 AAKKLTDKKggqygfALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEavealqfYVDLYKDGVAPSS----ATTG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 263 SDDWNAAFKSDTgFATIQCPAWLINNIKgNTGEDFQgWDIAdVFPGGGGNWGGSY-----LVVPESSPVKDEAAKLVAWL 337
Cdd:cd13585 219 GDEAVDLFASGK-VAMMIDGPWALGTLK-DSKVKFK-WGVA-PLPAGPGGKRASVlggwgLAISKNSKHPEAAWKFIKFL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 338 TEADQQVSVFTTAnnyPSSEGAQASSDVSSKTDTYLNDAPTGKIFANRAKAYDIVPYKGSQYFDIQTKMVDALNRVdatQ 417
Cdd:cd13585 295 TSKENQLKLGGAA---GPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGA---L 368
|
410
....*....|....*
gi 2519265878 418 EQTPDQAWKQWLEDV 432
Cdd:cd13585 369 GKSPEEALKEAAKEI 383
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
65-424 |
5.59e-21 |
|
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: 93.92 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 65 AKYEKAHPNVKIEETAAASSDDARAaFNTAISTGsNAYDVyvAEV--DWMPSLLAMpDKFVDLSSYTKDND----WVAWK 138
Cdd:cd14747 21 DEFEKENPGIEVKVQVLPWGDAHTK-ITTAAASG-DGPDV--VQLgnTWVAEFAAM-GALEDLTPYLEDLGgdkdLFPGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 139 SESATVDGKLIGAGTDIGPEGICYRADLLEKAGFPSDREsvaewlggddaTWDSFFKAGKEYTEKTG------LPWYDSM 212
Cdd:cd14747 96 VDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPK-----------TWDELEAAAKKIKADGPdvsgfaIPGKNDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 213 ASNWQSMINQVEESYVSKDDKIIAADNAKIKD---LYDQLTATKDMSAHLTQWSDDWNAAFKSDTGFATIQCPaWLINNI 289
Cdd:cd14747 165 WHNALPFVWGAGGDLATKDKWKATLDSPEAVAgleFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGP-WEIGAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 290 KGNTGEDFQGWDIAdVFPGGGGNWGGSY-----LVVPESSPVKDEAAKLVAWLTEADQQVSVFTTANNYPssegaqasSD 364
Cdd:cd14747 244 REAGPDLAGKWGVA-PLPGGPGGGSPSFaggsnLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLP--------AN 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519265878 365 VSSKTDTYLNDAPTGKIFAN---RAKAYDIVPykgsQYFDIQTKMVDALNRVDATQEQTPDQA 424
Cdd:cd14747 315 TSAWDDPSLANDPLLAVFAEqlkTGKATPATP----EWGEIEAELVLVLEEVWIGVGADVEDA 373
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
65-424 |
5.16e-19 |
|
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: 88.12 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 65 AKYEKAHPNVKIEETAAASSDDARAAFNTAISTGsNAYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDW-------VAW 137
Cdd:cd14748 21 DEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAG-TAPDVAQVDASWVAQLADS-GALEPLDDYIDKDGVddddfypAAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 138 ksESATVDGKLIGAGTDIGPEGICYRADLLEKAGFPSDREsvaewlggdDATWDSFFKAGKEYTEKTGL-------PWYD 210
Cdd:cd14748 99 --DAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKP---------PKTWDELEEAAKKLKDKGGKtgrygfaLPPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 211 SMASNWQSMINQVEESYVSKDDKIIAADNAKIKDLYDQLT--ATKDMSAHLTQWSDDWNaAFKSDTGFATIQCPaWLINN 288
Cdd:cd14748 168 DGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVdlVGKDGVSPLNDWGDAQD-AFISGKVAMTINGT-WSLAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 289 IKgNTGEDFQgWDIAdVFPGGGGNWGGSY-----LVVPESSP-VKDEAAKLVAWLTEADQQVsVFTTANNYPSsegaqAS 362
Cdd:cd14748 246 IR-DKGAGFE-YGVA-PLPAGKGKKGATPaggasLVIPKGSSkKKEAAWEFIKFLTSPENQA-KWAKATGYLP-----VR 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519265878 363 SDVSSKTDTYLNDAPTGKIFANRAKAYDIVPYKGSQYFDIQTKMVDALNRVdATQEQTPDQA 424
Cdd:cd14748 317 KSAAEDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAA-LLGKKTPEEA 377
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
62-367 |
3.11e-18 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 84.38 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 62 DLWAKYEKAHpNVKIEETAAASSDDARAaFNTAISTGSN-AYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDWVAWKsE 140
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQASNDLQAK-LLAAAAAGNApDLDVVWIAADQLATLAEA-GLLADLSDVDNLDDLPDAL-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 141 SATVDGKLIGAGTDIG-PEGICYRADLLEKAGfpsdresvaewlgGDDATWDSFFKAGKEYTEKTGlpWYDSmASNWQSM 219
Cdd:pfam13416 77 AAGYDGKLYGVPYAAStPTVLYYNKDLLKKAG-------------EDPKTWDELLAAAAKLKGKTG--LTDP-ATGWLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 220 INQVEESYVSKDDKiiaaDNAKIKDLYDQLTATKDMSAHlTQWSDDWNAAFKSDTgFATIQCPAWLINNIKGNtgedfqG 299
Cdd:pfam13416 141 ALLADGVDLTDDGK----GVEALDEALAYLKKLKDNGKV-YNTGADAVQLFANGE-VAMTVNGTWAAAAAKKA------G 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519265878 300 WDIADVFPGGGGNWGGSYLVVPESSPVKDEAA-KLVAWLTEADQQVSVFTTANNYPSSEGAQASSDVSS 367
Cdd:pfam13416 209 KKLGAVVPKDGSFLGGKGLVVPAGAKDPRLAAlDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKA 277
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-435 |
6.37e-14 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 73.06 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 1 MNKfKPALASVMALAMIVGLGACGSSNSSSDSSSADG-KITIKVQTfnnpgfgkPTSERPG-ADLWAKYEKAhPNVKIEE 78
Cdd:COG2182 1 MKR-RLLAALALALALALALAACGSGSSSSGSSSAAGaGGTLTVWV--------DDDEAEAlEEAAAAFEEE-PGIKVKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 79 TAAASSDDARAaFNTAISTGsNAYDVYVAEVDWMPS------LLAMPDKFVDLSSYTKdndwVAWksESATVDGKLIGAG 152
Cdd:COG2182 71 VEVPWDDLREK-LTTAAPAG-KGPDVFVGAHDWLGElaeaglLAPLDDDLADKDDFLP----AAL--DAVTYDGKLYGVP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 153 TDIGPEGICYRADLLEKAgfpsdresvaewlggDDATWDSFFKAGKEYTEKT----GLPWYDS------MASNWQSMINQ 222
Cdd:COG2182 143 YAVETLALYYNKDLVKAE---------------PPKTWDELIAAAKKLTAAGkyglAYDAGDAyyfypfLAAFGGYLFGK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 223 VEEsyvskDDKIIAADNAK-------IKDLYDQLTATKDMSAhltqwsDDWNAAFKSDTGFATIQCPaWLINNIKGNTGE 295
Cdd:COG2182 208 DGD-----DPKDVGLNSPGavaaleyLKDLIKDGVLPADADY------DAADALFAEGKAAMIINGP-WAAADLKKALGI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 296 DFqgwdIADVFPGGGGNWGGSY------LVVPESSPVKDEAAKLVAWLTEADQQVSVFTTANNYPSSEGAQASSDVSS-- 367
Cdd:COG2182 276 DY----GVAPLPTLAGGKPAKPfvgvkgFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKAdp 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519265878 368 KTDTYLNDAPTGKIFANrakaydiVPYkGSQYFDIqtkMVDALNRVdATQEQTPDQAWKQWLEDVKAL 435
Cdd:COG2182 352 LIAAFAEQAEYAVPMPN-------IPE-MGAVWTP---LGTALQAI-ASGKADPAEALDAAQKQIEAA 407
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
63-343 |
3.32e-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: 63.97 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 63 LWAKYEKAHPNVKIEeTAAASSDDARAAFNTAISTGSNAYDVYVAEVDWMPsLLAMPDKFVDLSSYTKDNDwvawksesA 142
Cdd:pfam01547 13 LVKEFEKEHPGIKVE-VESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIA-ELAKAGLLLPLDDYVANYL--------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 143 TVDGKLIGAGTDIGPEGICYRADLLEKAGFPsdresvaewlggDDATWDSFFKAGKEYTEKTGLPWYDSMASNW------ 216
Cdd:pfam01547 83 LGVPKLYGVPLAAETLGLIYNKDLFKKAGLD------------PPKTWDELLEAAKKLKEKGKSPGGAGGGDASgtlgyf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 217 -QSMINQVEESYVSKDDKIIAADNAK-----IKDLYDQLTATKDMSAHLTQWSDdWNAAFKSdtgFATIQCPAWLIN--- 287
Cdd:pfam01547 151 tLALLASLGGPLFDKDGGGLDNPEAVdaityYVDLYAKVLLLKKLKNPGVAGAD-GREALAL---FEQGKAAMGIVGpwa 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519265878 288 -----------NIKGNTGEDFQGWDIADVFPGGGGNWGGSYLVVPESSPVKDEAAKLVAWLTEADQQ 343
Cdd:pfam01547 227 alaankvklkvAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
67-428 |
4.24e-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: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 67 YEKAHPNVKIEETAAASSDDARAaFNTAIStGSNAYDVYVAEVDWMPSLLAMpDKFVDLSSYTKDNDWVAW---KSESAT 143
Cdd:cd14751 23 FEKEYPKIKVKAVRVPFDGLHNQ-IKTAAA-GGQAPDVMRADIAWVPEFAKL-GYLQPLDGTPAFDDIVDYlpgPMETNR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 144 VDGKLIGAGTDIGPEGICYRADLLEKAG--FPsdresvaewlggddATWDSFF---KAGKEYTEKTGLPWYDSMASNWQS 218
Cdd:cd14751 100 YNGHYYGVPQVTNTLALFYNKRLLEEAGteVP--------------KTMDELVaaaKAIKKKKGRYGLYISGDGPYWLLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 219 MINQVEESYVSKDDKIIAADNA-------KIKDLYDQLTATKDMSahlTQWSDDWNAaFKSDTGFATIQCPaWLINNIKG 291
Cdd:cd14751 166 FLWSFGGDLTDEKKATGYLNSPesvraleTIVDLYDEGAITPCAS---GGYPNMQDG-FKSGRYAMIVNGP-WAYADILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 292 NTG-EDFQGWDIADVfPGGGGNWGGSY----LVVPESSPVKDEAAKLVAWLTEADQQVSVFTTANNYPSSEGAQASSDVS 366
Cdd:cd14751 241 GKEfKDPDNLGIAPV-PAGPGGSGSPVggedLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519265878 367 sktdtylnDAPTGKIFA---NRAKAYDIVPYKGSQYFDIQTKMVDALnRVDATQEQTPDQAWKQW 428
Cdd:cd14751 320 --------NNPMVAAFKpalETAVPRPPIPEWGELFEPLTLAFAKVL-RGEKSPREALDEAAKQW 375
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
40-223 |
1.17e-07 |
|
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: 53.54 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 40 TIKVQTFNNPGFGKPTSErpgaDLWAKYEKAHPNVKIEETaAASSDDARAAFNTAISTGsNAYDVYVAEVDWMPSLLAMP 119
Cdd:cd14749 1 TITYWQYFTGDTKKKYMD----ELIADFEKENPNIKVKVV-VFPYDNYKTKLKTAVAAG-EGPDVFNLWPGGWLAEFVKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 120 DKFVDLSSYTKDNDWvaWKS------ESATVDGKLIGAGTDIGPEGICYRADLLEKAgfpsdresvaewlGGDD--ATWD 191
Cdd:cd14749 75 GLLLPLTDYLDPNGV--DKRflpglaDAVTFNGKVYGIPFAARALALFYNKDLFEEA-------------GGVKppKTWD 139
|
170 180 190
....*....|....*....|....*....|....
gi 2519265878 192 SFFKAGKEYTEKTGL--PWYDSMASNWQSMINQV 223
Cdd:cd14749 140 ELIEAAKKDKFKAKGqtGFGLLLGAQGGHWYFQY 173
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
55-208 |
2.14e-07 |
|
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: 52.68 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 55 TSERPGADLWAK----YEKAHPNVKIE-ETAAASSDDARAAFNTAISTGSNAYDVYVAEVDWMPSLLAmpdKFVDLSSYT 129
Cdd:cd14750 7 GSDGQEGELLKKaiaaFEKKHPDIKVEiEELPASSDDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAE---AGWLLPLTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 130 KDNDWVAWKS-----ESATVDGKLIG--AGTDIGpeGICYRADLLEKAGfpsdresvaewlGGDDATWDSFFKAGKEYTE 202
Cdd:cd14750 84 YLKEEEDDDFlpatvEANTYDGKLYAlpWFTDAG--LLYYRKDLLEKYG------------PEPPKTWDELLEAAKKRKA 149
|
....*.
gi 2519265878 203 KTGLPW 208
Cdd:cd14750 150 GEPGIW 155
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
65-427 |
1.30e-05 |
|
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: 47.02 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 65 AKYEKAHPNVKIEETaaASSDDARAAFNTAISTGSNAYDVYVAEVDWMPSLLAMP-----DKFVDLSSYTKDNDWVAWKs 139
Cdd:cd13522 21 AKFEKAYPGITVEVT--YQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGllaplDEYVSKSGKYAPNTIAAMK- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 140 esatVDGKLIGAGTDIGPEGICYRADLLEKAgfPSdresvaewlggddATWDSFFKAGKEytektglpwyDSMASNWQSM 219
Cdd:cd13522 98 ----LNGKLYGVPVSVGAHLMYYNKKLVPKN--PP-------------KTWQELIALAQG----------LKAKNVWGLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 220 INQVEE-----------SYVSKDD---KIIAADNAKIKDLYDQLTATKDMSAHLTQWSDD--WNAAFKSDTGFATIQCPa 283
Cdd:cd13522 149 YNQNEPyffaawiggfgGQVFKANngkNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYsiADALFKAGKAAMIINGP- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519265878 284 WLINNIKGNTGEDFqGWDIADVFPGGGGNW---GGSYLVVPESSPVKDEAAKLVAWLTEADQQVSVFTTANNYPSSEGAQ 360
Cdd:cd13522 228 WDLGDYRQALKINL-GVAPLPTFSGTKHAApfvGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAY 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519265878 361 ASSDVSSKT--DTYLNDAPTGKIFANrakaydiVPYKgSQYFDIqtkMVDALNRVDATQeQTPDQAWKQ 427
Cdd:cd13522 307 ESPAVQNKPaqKASAEQAAYGVPMPN-------IPEM-RAVWDA---FRIAVNSVLAGK-VTPEAAAKD 363
|
|
| |
