|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
47-415 |
1.29e-83 |
|
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: 261.46 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIAR-KMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKA 125
Cdd:cd14748 1 EITFWHGMSGPDGKALE-ELVDEFNKSHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEw 205
Cdd:cd14748 80 DDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGYVFTGTF---EFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWN 282
Cdd:cd14748 159 RYGFALPPGDggwTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 283 GVWQTTN--TAFDKLKWQAVAVPQIGDEK-AVWSSSthWMFMNNKGQDKNKtAAAATFVKWM--NDNSADWPK-TGELPA 356
Cdd:cd14748 239 GTWSLAGirDKGAGFEYGVAPLPAGKGKKgATPAGG--ASLVIPKGSSKKK-EAAWEFIKFLtsPENQAKWAKaTGYLPV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 357 KNSVRDDPK-LVQTYPNLKPFLDELPYAHYE-PIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14748 316 RKSAAEDPEeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEE 376
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
8-341 |
8.72e-68 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 219.92 E-value: 8.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 8 RAIAVAVTAGLGLALTACGSSSSGGGGDvssadytGPKVTISFWngWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWA 87
Cdd:COG1653 2 RRLALALAAALALALAACGGGGSGAAAA-------AGKVTLTVW--HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:COG1653 73 DYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGvqGEWvdGYVFTGT--FEFESLLWQYGGDLFNKDvSKATFNSDAGVK 245
Cdd:COG1653 153 NKDLFEKAGLDP---PKTWDELLAAAKKLKAKD--GVY--GFALGGKdgAAWLDLLLSAGGDLYDED-GKPAFDSPEAVE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 246 ALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAFNWNGVWQTTN--TAFDKLKWQAVAVPQI--GDEKAVWSSSTHW 318
Cdd:COG1653 225 ALEFLKDLVKDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGAlkDAAPDFDVGVAPLPGGpgGKKPASVLGGSGL 304
|
330 340
....*....|....*....|...
gi 1085662500 319 MFMNNKgqdKNKtAAAATFVKWM 341
Cdd:COG1653 305 AIPKGS---KNP-EAAWKFLKFL 323
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
65-373 |
5.71e-25 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 103.64 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAV--GHGDDIATYAAQGLVLKADSIVKSlgykaDDFPEg 142
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNL-----DDLPD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 LLDAGKYNGSQYAVPWSI-TPLGLYVNKDVLQAAGVDPNSIpqdkDSYLAALEKLKAAGVQGEWVDGYVFTGtfefeslL 221
Cdd:pfam13416 74 ALDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAGEDPKTW----DELLAAAAKLKGKTGLTDPATGWLLWA-------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 222 WQYGGDLFNKDVSKatfnsDAGVKALTWMTDLIKKGYSPAdvAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVa 301
Cdd:pfam13416 143 LADGVDLTDDGKGV-----EALDEALAYLKKLKDNGKVYN--TGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085662500 302 VPQIGdekAVWSSSTHWMFmnnkGQDKNKTAAAATFVKWMN--DNSADWPK-TGELPAKNSVRDDPKlVQTYPNL 373
Cdd:pfam13416 215 VPKDG---SFLGGKGLVVP----AGAKDPRLAALDFIKFLTspENQAALAEdTGYIPANKSAALSDE-VKADPAL 281
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
92-289 |
1.65e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 50.01 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 92 KMPLAVKAGKGPDVAVGHGDDIATYAAQGLV--LKADSIVKSlgyKADDFPeglLDAGKYNGSQYAVPWSITPLGLYVNK 169
Cdd:PRK09474 72 KFPQVAATGDGPDIIFWAHDRFGGYAQSGLLaeVTPSKAFKD---KLVPFT---WDAVRYNGKLIGYPIAVEALSLIYNK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 170 DVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQG-EW-VDGYVFTGtfefeSLLWQYGGDLFNK-----DVSKATFNSDA 242
Cdd:PRK09474 146 DLVPTP-------PKTWEEIPALDKELKAKGKSAiMWnLQEPYFTW-----PLIAADGGYAFKFenggyDVKDVGVNNAG 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1085662500 243 GVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN 289
Cdd:PRK09474 214 AKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSN 260
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
47-415 |
1.29e-83 |
|
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: 261.46 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIAR-KMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKA 125
Cdd:cd14748 1 EITFWHGMSGPDGKALE-ELVDEFNKSHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEw 205
Cdd:cd14748 80 DDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGYVFTGTF---EFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWN 282
Cdd:cd14748 159 RYGFALPPGDggwTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 283 GVWQTTN--TAFDKLKWQAVAVPQIGDEK-AVWSSSthWMFMNNKGQDKNKtAAAATFVKWM--NDNSADWPK-TGELPA 356
Cdd:cd14748 239 GTWSLAGirDKGAGFEYGVAPLPAGKGKKgATPAGG--ASLVIPKGSSKKK-EAAWEFIKFLtsPENQAKWAKaTGYLPV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 357 KNSVRDDPK-LVQTYPNLKPFLDELPYAHYE-PIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14748 316 RKSAAEDPEeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEE 376
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
8-341 |
8.72e-68 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 219.92 E-value: 8.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 8 RAIAVAVTAGLGLALTACGSSSSGGGGDvssadytGPKVTISFWngWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWA 87
Cdd:COG1653 2 RRLALALAAALALALAACGGGGSGAAAA-------AGKVTLTVW--HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:COG1653 73 DYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGvqGEWvdGYVFTGT--FEFESLLWQYGGDLFNKDvSKATFNSDAGVK 245
Cdd:COG1653 153 NKDLFEKAGLDP---PKTWDELLAAAKKLKAKD--GVY--GFALGGKdgAAWLDLLLSAGGDLYDED-GKPAFDSPEAVE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 246 ALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAFNWNGVWQTTN--TAFDKLKWQAVAVPQI--GDEKAVWSSSTHW 318
Cdd:COG1653 225 ALEFLKDLVKDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGAlkDAAPDFDVGVAPLPGGpgGKKPASVLGGSGL 304
|
330 340
....*....|....*....|...
gi 1085662500 319 MFMNNKgqdKNKtAAAATFVKWM 341
Cdd:COG1653 305 AIPKGS---KNP-EAAWKFLKFL 323
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-415 |
1.37e-62 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 207.88 E-value: 1.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 1 MKKRFAAraiAVAVTAGLGLALTACGSSSSGGGGDVSSADytGPKVTIsfwngWTGGAAPVLVPKLIDKFNSEHkNIVVK 80
Cdd:COG2182 1 MKRRLLA---ALALALALALALAACGSGSSSSGSSSAAGA--GGTLTV-----WVDDDEAEALEEAAAAFEEEP-GIKVK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 81 DVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSlgykADDFPEGLLDAGKYNGSQYAVPWSI 160
Cdd:COG2182 70 VVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLAD----KDDFLPAALDAVTYDGKLYGVPYAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 161 TPLGLYVNKDVLqaagvdPNSIPQDKDSYLAALEKLKAAGVQGEWVDgyvFTGTFEFESLLWQYGGDLFNK---DVSKAT 237
Cdd:COG2182 146 ETLALYYNKDLV------KAEPPKTWDELIAAAKKLTAAGKYGLAYD---AGDAYYFYPFLAAFGGYLFGKdgdDPKDVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 238 FNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN-TAFDKLKWQAVAVPQI--GDEKAVWSS 314
Cdd:COG2182 217 LNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADlKKALGIDYGVAPLPTLagGKPAKPFVG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 315 STHWMFMNNKgqdKNKTAAAAtFVKWMNDNSAD---WPKTGELPAKNSVRDDPKlVQTYPNLKPFLDELPYAHYEPIAPG 391
Cdd:COG2182 297 VKGFGVSAYS---KNKEAAQE-FAEYLTSPEAQkalFEATGRIPANKAAAEDAE-VKADPLIAAFAEQAEYAVPMPNIPE 371
|
410 420
....*....|....*....|....
gi 1085662500 392 ITTVEATITVAVNEAITGKKDPKQ 415
Cdd:COG2182 372 MGAVWTPLGTALQAIASGKADPAE 395
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
47-415 |
1.10e-60 |
|
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: 202.25 E-value: 1.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVLvPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13585 1 TLTFWDWGQPAETAAL-KKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKaDDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnSIPQDKDSYLAALEKLKAAGVQgewV 206
Cdd:cd13585 80 DYIEKDGLD-DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGP-KPPWTWDELLEAAKKLTDKKGG---Q 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 DGYVFTG----TFEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGN--INALIAGKTAFN 280
Cdd:cd13585 155 YGFALRGgsggQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDeaVDLFASGKVAMM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 281 WNGVWQ--TTNTAFDKLKWQAVAVPQIGDEKAVWSSSTHWMFMNNKGQDKnktAAAATFVKWM----NDNSADWPKTGEL 354
Cdd:cd13585 235 IDGPWAlgTLKDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHP---EAAWKFIKFLtskeNQLKLGGAAGPAA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085662500 355 PAKNSVRDDPKLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGK--KDPKQ 415
Cdd:cd13585 312 LAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEE 374
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
47-415 |
3.74e-53 |
|
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: 182.58 E-value: 3.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVA-VGHGDDIATYAAQGLVLKA 125
Cdd:cd14749 1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKaDDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGvdPNSIPQDKDSYLAALEKLKAA--GVQG 203
Cdd:cd14749 81 TDYLDPNGVD-KRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKakGQTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 204 EWVDGYVFTGTFEFESLLWQYGGDLFNKDVS-KATFNSDAGVKALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAF 279
Cdd:cd14749 158 FGLLLGAQGGHWYFQYLVRQAGGGPLSDDGSgKATFNDPAFVQALQKLQDLVKAGAFQEGFEGidyDDAGQAFAQGKAAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 280 NWNGVWQTTN--TAFDKLKWQAVAVPQIGdEKAVWSSS--THWMFMNNKGQDknKTAAAATFVKWMNDNSAD---WPKTG 352
Cdd:cd14749 238 NIGGSWDLGAikAGEPGGKIGVFPFPTVG-KGAQTSTIggSDWAIAISANGK--KKEAAVKFLKYLTSPEVMkqyLEDVG 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 353 ELPAKNSVRDDPKLVQtYPNLKPFLDELPYAHYEPIA-PGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14749 315 LLPAKEVVAKDEDPDP-VAILGPFADVLNAAGSTPFLdEYWPAAAQVHKDAVQKLLTGKIDPEQ 377
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
47-415 |
9.48e-48 |
|
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: 167.88 E-value: 9.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWtGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGlVLKAD 126
Cdd:cd14747 1 TLTVWAMG-NSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMG-ALEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGvdPNSIPQDKDSYLAALEKLKAagvQGEWV 206
Cdd:cd14747 79 TPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKA---DGPDV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 DGYVFTGT----FEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDG-NINALIA-GKTAFN 280
Cdd:cd14747 154 SGFAIPGKndvwHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSaDVEQAFAnGKVAMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 281 WNGVWQ----TTNTAFDKLKWQAVAVP-QIGDEKAVWSSSTHWMFMNNKgqdKNKTAAAAtFVKWM--NDNSADWPK-TG 352
Cdd:cd14747 234 ISGPWEigaiREAGPDLAGKWGVAPLPgGPGGGSPSFAGGSNLAVFKGS---KNKDLAWK-FIEFLssPENQAAYAKaTG 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 353 ELPAKNSVRDDPKLVQTyPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITG-KKDPKQ 415
Cdd:cd14747 310 MLPANTSAWDDPSLAND-PLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVED 372
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
65-415 |
1.74e-44 |
|
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: 159.38 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 65 KLIDKFNSEHKNIVVKDVPMEW-ADIARKMPLAVKAGKGPDVAVGHGDDI--ATYAAQGLVLKADSIVKSLGYkaDDFPE 141
Cdd:cd14750 18 KAIAAFEKKHPDIKVEIEELPAsSDDQRQQLVTALAAGSSAPDVLGLDVIwiPEFAEAGWLLPLTEYLKEEED--DDFLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 142 GLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEKLKAagvQGEWVDGYVFTG-TFE---- 216
Cdd:cd14750 96 ATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEP---PKTWDELLEAAKKRKA---GEPGIWGYVFQGkQYEglvc 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 217 -FESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADV---AQDGNINALIAGKTAF--NWNGVWQTTNT 290
Cdd:cd14750 170 nFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGVltyGEEEARAAFQAGKAAFmrNWPYAYALLQG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 291 AFDKL--KWQAVAVPQIGDEKAVwSSSTHWMFMNNKgQDKNKtAAAATFVKWMNdnSADWPKT-----GELPAKNSVRDD 363
Cdd:cd14750 250 PESAVagKVGVAPLPAGPGGGSA-STLGGWNLAISA-NSKHK-EAAWEFVKFLT--SPEVQKRraingGLPPTRRALYDD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1085662500 364 PKLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14750 325 PEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEE 376
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
47-415 |
6.20e-36 |
|
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: 135.97 E-value: 6.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGwTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd14751 1 TITFWHT-SSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVksLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEK-LKAAGVQGEW 205
Cdd:cd14751 80 GTP--AFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEV---PKTMDELVAAAKAiKKKKGRYGLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGyvfTGTFEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYS--PADVAQDGNINALIAGKTAFNWNG 283
Cdd:cd14751 155 ISG---DGPYWLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAItpCASGGYPNMQDGFKSGRYAMIVNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 284 VWQTTN-----TAFDKLKWQAVAVPQ--------IGDEKAVwsssthwMFMNNKGQDknktaAAATFVKWMNDNSADWPK 350
Cdd:cd14751 232 PWAYADilggkEFKDPDNLGIAPVPAgpggsgspVGGEDLV-------IFKGSKNKD-----AAWKFVKFMSSAEAQALT 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085662500 351 TGE---LPAKNSVRDDPKLVQTyPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14751 300 AAKlglLPTRTSAYESPEVANN-PMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPRE 366
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
47-415 |
8.67e-30 |
|
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: 119.02 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13657 1 TITIWHALTGAEEDALQ-QIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLgyKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQGEwv 206
Cdd:cd13657 80 DYLSED--DFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQP-------PETTDELLAIMKDHTDPAAGSY-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 dGYVFT-GTFEFESLLWQ-YGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKgYSPADVAQDGNINALIAGKTAFNWNGV 284
Cdd:cd13657 149 -GLAYQvSDAYFVSAWIFgFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWP-YMPSDPSYNTQTSLFNEGKAAMIINGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 285 WQTTNTAFDKLKWQAVAVPQIGDEKAVWSSSTHWMFMNNKGQDKNKTAAAATFVKWMNDNS-----ADwpKTGELPAKNS 359
Cdd:cd13657 227 WFIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEaskilAD--ENGYVPAATN 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1085662500 360 VRDDPKlVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13657 305 AYDDAE-VAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQE 359
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
47-415 |
1.08e-29 |
|
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: 118.55 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNGWTGGAAPVlvPKLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13586 1 TITVWTDEDGELEYL--KELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKslgyKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLqaagVDPnsiPQDKDSYLAALEK--LKAAGVQG- 203
Cdd:cd13586 78 EYLA----VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLV----PEP---PKTWEELIALAKKfnDKAGGKYGf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 204 --EWVDGYVFTGtfefesLLWQYGGDLF---NKDVSKATFNSDAGVKALTWMTDLIKK-GYSPADVAQDGNINALIAGKT 277
Cdd:cd13586 147 ayDQTNPYFSYP------FLAAFGGYVFgenGGDPTDIGLNNEGAVKGLKFIKDLKKKyKVLPPDLDYDIADALFKEGKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 278 AFNWNGVWQTTNTAFDKLKWQAVAVPQIgdEKAVWS---SSTHWMFMNNKGQDKnktAAAATFVKWMNDNSAD---WPKT 351
Cdd:cd13586 221 AMIINGPWDLADYKDAGINFGVAPLPTL--PGGKQAapfVGVQGAFVSAYSKNK---EAAVEFAEYLTSDEAQlllFEKT 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 352 GELPAKNSVRDDPkLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13586 296 GRIPALKDALNDA-AVKNDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEE 358
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
47-415 |
1.55e-26 |
|
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: 109.81 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 47 TISFWNgWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13522 1 TITVWH-QYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKADDFpeglLDAGKYNGSQYAVPWSITPLGLYVNKDVLqaagvdPNSIPQDKDSYLAALEKLKAAGVqgeWv 206
Cdd:cd13522 80 EYVSKSGKYAPNT----IAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKAKNV---W- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 dGYVFTGT--FEFESLLWQYGGDLF--NKDVSKATFNSDAGVKALTWMTDLIKK-GYSPADVAQDGNINALIAGKTAFNW 281
Cdd:cd13522 146 -GLVYNQNepYFFAAWIGGFGGQVFkaNNGKNNPTLDTPGAVEALQFLVDLKSKyKIMPPETDYSIADALFKAGKAAMII 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 282 NGVWqTTNTAFDKLKWQAVAVPQIGDEKAVWSS----STHWMfMNNKGQDKnktAAAATFVKWMNDNSAD---WPKTGEL 354
Cdd:cd13522 225 NGPW-DLGDYRQALKINLGVAPLPTFSGTKHAApfvgGKGFG-INKESQNK---AAAVEFVKYLTSYQAQlvlFDDAGDI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 355 PAKNSVRDDPkLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13522 300 PANLQAYESP-AVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEA 359
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
65-373 |
5.71e-25 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 103.64 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAV--GHGDDIATYAAQGLVLKADSIVKSlgykaDDFPEg 142
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNL-----DDLPD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 LLDAGKYNGSQYAVPWSI-TPLGLYVNKDVLQAAGVDPNSIpqdkDSYLAALEKLKAAGVQGEWVDGYVFTGtfefeslL 221
Cdd:pfam13416 74 ALDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAGEDPKTW----DELLAAAAKLKGKTGLTDPATGWLLWA-------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 222 WQYGGDLFNKDVSKatfnsDAGVKALTWMTDLIKKGYSPAdvAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVa 301
Cdd:pfam13416 143 LADGVDLTDDGKGV-----EALDEALAYLKKLKDNGKVYN--TGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085662500 302 VPQIGdekAVWSSSTHWMFmnnkGQDKNKTAAAATFVKWMN--DNSADWPK-TGELPAKNSVRDDPKlVQTYPNL 373
Cdd:pfam13416 215 VPKDG---SFLGGKGLVVP----AGAKDPRLAALDFIKFLTspENQAALAEdTGYIPANKSAALSDE-VKADPAL 281
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
65-415 |
2.25e-20 |
|
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: 92.16 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKadsiVKSLGYKADDFPEGLL 144
Cdd:cd13658 17 KIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSP----IKLSKDKKKGFTDQAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 145 DAGKYNGSQYAVPWSITPLGLYVNKDVLQAAgvdPNSIpQDKDSYLAAL--EKLKAAGVQGEWVDGYVFTGtfefesLLW 222
Cdd:cd13658 92 KALTYDGKLYGLPAAVETLALYYNKDLVKNA---PKTF-DELEALAKDLtkEKGKQYGFLADATNFYYSYG------LLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 223 QYGGDLFNK-----DVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKW 297
Cdd:cd13658 162 GNGGYIFKKngsdlDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVNY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 298 QAVAVPQIGDEKAVWSssthwmFMNNKG-----QDKNKtAAAATFVKWMN--DNSAD-WPKTGELPAKNSVRDDPkLVQT 369
Cdd:cd13658 242 GVAPLPTLPNGKPMAP------FLGVKGwylsaYSKHK-EWAQKFMEFLTskENLKKrYDETNEIPPRKDVRSDP-EIKN 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1085662500 370 YPNLKPFldELPYAHYEPIaPGITTVEATITVAVN---EAITGKKDPKQ 415
Cdd:cd13658 314 NPLTSAF--AKQASRAVPM-PNIPEMGAVWEPANNalfFILSGKKTPKQ 359
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
64-346 |
1.19e-16 |
|
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: 80.15 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 64 PKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGP-DVAVGHGDDIATYAAQGLVLKADSIVKSlgykaddfpeg 142
Cdd:pfam01547 11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVAN----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 llDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGVQGEWVDGYVFTGTFE--FESL 220
Cdd:pfam01547 80 --YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP---PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyfTLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 221 LWQYGGDLFNKDVskATFNSDAGVKALTWMTDLI--------KKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAF 292
Cdd:pfam01547 155 LASLGGPLFDKDG--GGLDNPEAVDAITYYVDLYakvlllkkLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 293 DKLKwQAVAVPQIGDEKAV----------WSSSTHWMFMNNKGQDKnktAAAATFVKWMNDNSA 346
Cdd:pfam01547 233 VKLK-VAFAAPAPDPKGDVgyaplpagkgGKGGGYGLAIPKGSKNK---EAAKKFLDFLTSPEA 292
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
88-305 |
1.82e-10 |
|
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: 62.23 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVlkadSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:cd13656 38 KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLL----AEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLqaagvdPNSiPQDKDSYLAALEKLKAAGVQGEWVDgyvFTGTFEFESLLWQYGGDLFNKDVSKaTFNSDAGV--- 244
Cdd:cd13656 114 NKDLL------PNP-PKTWEEIPALDKELKAKGKSALMFN---LQEPYFTWPLIAADGGYAFKYENGK-YDIKDVGVdna 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 245 ---KALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVAVPQI 305
Cdd:cd13656 183 gakAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTF 246
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
44-386 |
8.69e-08 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 54.26 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 44 PKVTISFWNGWTGGAAP-----VLVPKLIDKFNSEHKNIVVKDVpmEWADiarKMPLAVKAGKGPDVAVGHGDD-IATYA 117
Cdd:cd13580 1 EPVTITIVANLGGNPKPdpddnPYTKYLEEKTNIDVKVKWVPDS--SYDE---KLNLALASGDLPDIVVVNDPQlSITLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 118 AQGLVLKADSIVKSLG--YKADDFPEGLlDAGKYNGSQYAVPWS---ITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAA 192
Cdd:cd13580 76 KQGALWDLTDYLDKYYpnLKKIIEQEGW-DSASVDGKIYGIPRKrplIGRNGLWIRKDWLDKLGLEV---PKTLDELYEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 193 LEKLKAAGVQGEWV-DGYVFTGTFE-----FESLLWQYGG--DLFNKDVS---KATFNSDAGVKALTWMTDLIKKGYSPA 261
Cdd:cd13580 152 AKAFTEKDPDGNGKkDTYGLTDTKDligsgFTGLFGAFGAppNNWWKDEDgklVPGSIQPEMKEALKFLKKLYKEGLIDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 262 DVA--QDGNINALI-AGKTAF---NWNGVWQTTNTAFDKL---KWQAVAVPQIGD-EKAVWSSSTHW-MFMNNKGQDKNK 330
Cdd:cd13580 232 EFAvnDGTKANEKFiSGKAGIfvgNWWDPAWPQASLKKNDpdaEWVAVPIPSGPDgKYGVWAESGVNgFFVIPKKSKKPE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1085662500 331 taAAATFVKWMNDNSADWPKTGELPAKNSVRDDPKLVQTYPNLKPFLDELPYAHYE 386
Cdd:cd13580 312 --AILKLLDFLSDPEVQKLLDYGIEGVHYTVKDGGPVNIIPPDKQEVGDATLDYFQ 365
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
92-289 |
1.65e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 50.01 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 92 KMPLAVKAGKGPDVAVGHGDDIATYAAQGLV--LKADSIVKSlgyKADDFPeglLDAGKYNGSQYAVPWSITPLGLYVNK 169
Cdd:PRK09474 72 KFPQVAATGDGPDIIFWAHDRFGGYAQSGLLaeVTPSKAFKD---KLVPFT---WDAVRYNGKLIGYPIAVEALSLIYNK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 170 DVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQG-EW-VDGYVFTGtfefeSLLWQYGGDLFNK-----DVSKATFNSDA 242
Cdd:PRK09474 146 DLVPTP-------PKTWEEIPALDKELKAKGKSAiMWnLQEPYFTW-----PLIAADGGYAFKFenggyDVKDVGVNNAG 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1085662500 243 GVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN 289
Cdd:PRK09474 214 AKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSN 260
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
62-275 |
2.32e-05 |
|
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 46.18 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 62 LVPKLIDKFNSEHK--NIVVKDVPMEWADIARKmpLAVKAGKGPDVAVGHGDDIATYAAQGLVL----KADSIVKSlgyk 135
Cdd:cd13655 13 WLKEMVDAFKEKHPewKITITIGVVGEADAKDE--VLKDPSAAADVFAFANDQLGELVDAGAIYpltgSAVDKIKN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 136 adDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVdpnsipQDKDSYLAALEKLKAAgVQGEWVDGYVFTGTF 215
Cdd:cd13655 87 --TNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDV------KSLDTMLAKAPDAKGK-VSFDLSNSWYLYAFF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 216 efesllWQYGGDLF---NKDVSKATFNSDAGVKALTWMTDLI--KKGYSPAD-----VAQDGNINALIAG 275
Cdd:cd13655 158 ------FGAGCKLFgnnGGDTAGCDFNNEKGVAVTNYLVDLVanPKFVNDADgdaisGLKDGTLGAGVSG 221
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
5-257 |
5.71e-05 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 45.18 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 5 FAARAIAVAVTAGLGLALTACGSsssggggdvssadytgpkVTISFWNGWTGgAAPVLVPKLIDKFNSEHKNivVKDVPM 84
Cdd:PRK10974 3 KSLRSTALGLALGLALSGNAQAV------------------TEIPFWHSMEG-ELGKEVDSLAQRFNASQPD--YKIVPV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 85 EWADIARKMPL---AVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKY----NGSQYAVP 157
Cdd:PRK10974 62 YKGNYEQSLAAgiaAFRSGNAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYsdakTGHLLSQP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 158 W-SITPLgLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEWVDGYvfTGTFEFESLLWQYG------GDLFN 230
Cdd:PRK10974 142 FnSSTPV-LYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGYASGW--QGWIQLENFSAWHGlpfaskNNGFD 218
|
250 260
....*....|....*....|....*..
gi 1085662500 231 KDVSKATFNSDAGVKALTWMTDLIKKG 257
Cdd:PRK10974 219 GTDAVLEFNKPEQVKHIALLEEMNKKG 245
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1-199 |
5.08e-03 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 38.74 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 1 MKKRFAARAIAVAVTAGLGLALTAcgssssggggdvsSADytGPKVTISFWngwtGGAAPvlvPKLIDKFNSEHKNIVVK 80
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGGAPA-------------AAA--EGTLNVYNW----GGYID---PDVLEPFEKETGIKVVY 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 81 DVPMEWADIARKMplavKAGKGP-DVAVGHGDDIATYAAQGLVLKAD-SIVKSLGYKADDFPEGLLDAGKyngsQYAVPW 158
Cdd:COG0687 59 DTYDSNEEMLAKL----RAGGSGyDVVVPSDYFVARLIKAGLLQPLDkSKLPNLANLDPRFKDPPFDPGN----VYGVPY 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 159 SITPLGLYVNKDV---------------------------------LQAAGVDPNSIpqDKDSYLAALEKLKAA 199
Cdd:COG0687 131 TWGTTGIAYNTDKvkepptswadlwdpeykgkvallddprevlgaaLLYLGYDPNST--DPADLDAAFELLIEL 202
|
|
|