|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
89-479 |
1.58e-156 |
|
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: 450.71 E-value: 1.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVTYGVGVGTSQFETAAKAGQ-APIVYRDTSDSGGALFAAGLVLNLSQ 167
Cdd:cd13522 1 TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGkGPDVVFGPSDSLGPFAAAGLLAPLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 168 YLPQSVTslYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPYPPNTTEQLVQIAESVNKTYHVWGIAYGAGdeYGYR 247
Cdd:cd13522 81 YVSKSGK--YAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPKNPPKTWQELIALAQGLKAKNVWGLVYNQN--EPYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 248 FAAWFAGFGGQIFATNNGKIVPSLNSTAMVnaLNFWYNLTYNLKVNYLAPSTGaGGAEGQLFVANQTAIIFDGPWDLNAY 327
Cdd:cd13522 157 FAAWIGGFGGQVFKANNGKNNPTLDTPGAV--EALQFLVDLKSKYKIMPPETD-YSIADALFKAGKAAMIINGPWDLGDY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 328 LQALGPNLGAAPLPVVSQTgLRAAPFIGSTGFLIASPQAsgatqlQIKAALIFVLYFTNYQADLRLWEVAHDIPANLQAY 407
Cdd:cd13522 234 RQALKINLGVAPLPTFSGT-KHAAPFVGGKGFGINKESQ------NKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAY 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502107763 408 NEALTQLKEGMLQPtylnrimegiLEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGMEQAF 479
Cdd:cd13522 307 ESPAVQNKPAQKAS----------AEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
81-485 |
2.90e-93 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 290.31 E-value: 2.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 81 STAPSTPVTITVWnsYSTSENQAFNETLAQFEQAfPWIHVQV-TYGVGVGTSQFETAAKAGQAPIVYRDTSDSGGALFAA 159
Cdd:COG2182 32 SSAAGAGGTLTVW--VDDDEAEALEEAAAAFEEE-PGIKVKVvEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 160 GLVLNLSQYLpqSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPY-PPNTTEQLVQIAESVNKTyHVWGIAY 238
Cdd:COG2182 109 GLLAPLDDDL--ADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAePPKTWDELIAAAKKLTAA-GKYGLAY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 239 GAGDeyGYRFAAWFAGFGGQIFATN-NGKIVPSLNSTAMVNALNFWYNLTYNLkvnyLAPSTGAGGAEGQLFVANQTAII 317
Cdd:COG2182 186 DAGD--AYYFYPFLAAFGGYLFGKDgDDPKDVGLNSPGAVAALEYLKDLIKDG----VLPADADYDAADALFAEGKAAMI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 318 FDGPWDLNAYLQALGPNLGAAPLPVVsQTGLRAAPFIGSTGFLIASPQASGAtqlqikAALIFVLYFTNYQADLRLWEVA 397
Cdd:COG2182 260 INGPWAAADLKKALGIDYGVAPLPTL-AGGKPAKPFVGVKGFGVSAYSKNKE------AAQEFAEYLTSPEAQKALFEAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 398 HDIPANLQAYNEAltQLKEgmlqptylNRIMEGILEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGMEQ 477
Cdd:COG2182 333 GRIPANKAAAEDA--EVKA--------DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQK 402
|
....*...
gi 502107763 478 AFIQALVQ 485
Cdd:COG2182 403 QIEAAIAQ 410
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
130-454 |
1.42e-13 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 72.35 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 130 TSQFETAAKAGQAPIVYRDTSDSGGALFAAGLvlnLSQYLP-QSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK 208
Cdd:PRK09474 70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGL---LAEVTPsKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 209 FVPYPPNTTEQLVQIAESVNK------------TYHVWGIaygagdeygyrfaawFAGFGGQIFATNNGKIVPS---LNS 273
Cdd:PRK09474 147 LVPTPPKTWEEIPALDKELKAkgksaimwnlqePYFTWPL---------------IAADGGYAFKFENGGYDVKdvgVNN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 274 TAMVNALNFWYNLtynLKVNYLAPSTGAGGAEGQlFVANQTAIIFDGPWDLnAYLQALGPNLGAAPLPVVsqTGLRAAPF 353
Cdd:PRK09474 212 AGAKAGLQFLVDL---VKNKHMNADTDYSIAEAA-FNKGETAMTINGPWAW-SNIDKSGINYGVTVLPTF--NGKPSKPF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 354 IG--STGFLIASPQASGATQlqikaalifvlYFTNYQ-ADLRLWEVAHDIP---ANLQAYNEALTqlKEGMLQPTYLNri 427
Cdd:PRK09474 285 VGvlSAGINAASPNKELAKE-----------FLENYLlTDEGLETVNKDKPlgaVALKSFQEELA--KDPRIAATMDN-- 349
|
330 340
....*....|....*....|....*..
gi 502107763 428 megileqAQYGQQFPNIPQMAYYWNSF 454
Cdd:PRK09474 350 -------AQNGEIMPNIPQMSAFWYAM 369
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
109-410 |
1.65e-10 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 62.04 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 109 AQFEQAFPWIHVQVTYGVGVGTSQFETAAKAGQAP--IVYRDTSDSGGALFAAGLVLNLSQYlpqsVTSLYVPTAIKDWE 186
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPdlDVVWIAADQLATLAEAGLLADLSDV----DNLDDLPDALDAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 187 LNGSLYGLPDNVNY-IVMFYNKKFVP---YPPNTTEQLVQIAESV--NKTYHVWGIAYgagdeygYRFAAWFAGfggqif 260
Cdd:pfam13416 80 YDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLkgKTGLTDPATGW-------LLWALLADG------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 261 ATNNGKIVPSLNSTAmvnALNFWYNLTYNLKVnylaPSTGAGGAegQLFVANQTAIIFDGPWDLNAYLQAlGPNLGAAPL 340
Cdd:pfam13416 147 VDLTDDGKGVEALDE---ALAYLKKLKDNGKV----YNTGADAV--QLFANGEVAMTVNGTWAAAAAKKA-GKKLGAVVP 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 341 PvvsqtglrAAPFIGSTGFLIaspqASGATQLQIkAALIFVLYFTNYQADLRLWEVAHDIPANLQAYNEA 410
Cdd:pfam13416 217 K--------DGSFLGGKGLVV----PAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKSAALSD 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
89-479 |
1.58e-156 |
|
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: 450.71 E-value: 1.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVTYGVGVGTSQFETAAKAGQ-APIVYRDTSDSGGALFAAGLVLNLSQ 167
Cdd:cd13522 1 TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGkGPDVVFGPSDSLGPFAAAGLLAPLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 168 YLPQSVTslYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPYPPNTTEQLVQIAESVNKTYHVWGIAYGAGdeYGYR 247
Cdd:cd13522 81 YVSKSGK--YAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPKNPPKTWQELIALAQGLKAKNVWGLVYNQN--EPYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 248 FAAWFAGFGGQIFATNNGKIVPSLNSTAMVnaLNFWYNLTYNLKVNYLAPSTGaGGAEGQLFVANQTAIIFDGPWDLNAY 327
Cdd:cd13522 157 FAAWIGGFGGQVFKANNGKNNPTLDTPGAV--EALQFLVDLKSKYKIMPPETD-YSIADALFKAGKAAMIINGPWDLGDY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 328 LQALGPNLGAAPLPVVSQTgLRAAPFIGSTGFLIASPQAsgatqlQIKAALIFVLYFTNYQADLRLWEVAHDIPANLQAY 407
Cdd:cd13522 234 RQALKINLGVAPLPTFSGT-KHAAPFVGGKGFGINKESQ------NKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAY 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502107763 408 NEALTQLKEGMLQPtylnrimegiLEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGMEQAF 479
Cdd:cd13522 307 ESPAVQNKPAQKAS----------AEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
89-479 |
1.29e-117 |
|
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: 351.21 E-value: 1.29e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTsENQAFNETLAQFEQAFpWIHVQVTYGVGVGTSQ-FETAAKAGQAPIVYRDTSDSGGALFAAGLVLNLSQ 167
Cdd:cd13586 1 TITVWTDEDG-ELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREkFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 168 YLPQSVtsLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPYPPNTTEQLVQIAES-VNKTYHVWGIAYGAGDeyGY 246
Cdd:cd13586 79 YLAVKI--KNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKKfNDKAGGKYGFAYDQTN--PY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 247 RFAAWFAGFGGQIFATNN-GKIVPSLNSTAMVNALNFWYNLtyNLKVNYLAPSTGAGGAeGQLFVANQTAIIFDGPWDLN 325
Cdd:cd13586 155 FSYPFLAAFGGYVFGENGgDPTDIGLNNEGAVKGLKFIKDL--KKKYKVLPPDLDYDIA-DALFKEGKAAMIINGPWDLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 326 AYlQALGPNLGAAPLPVVSQtGLRAAPFIGSTGFLIASPQAsgatqlQIKAALIFVLYFTNYQADLRLWEVAHDIPANLQ 405
Cdd:cd13586 232 DY-KDAGINFGVAPLPTLPG-GKQAAPFVGVQGAFVSAYSK------NKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKD 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502107763 406 AYNEALTQlkegmlqptyLNRIMEGILEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGMEQAF 479
Cdd:cd13586 304 ALNDAAVK----------NDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
81-485 |
2.90e-93 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 290.31 E-value: 2.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 81 STAPSTPVTITVWnsYSTSENQAFNETLAQFEQAfPWIHVQV-TYGVGVGTSQFETAAKAGQAPIVYRDTSDSGGALFAA 159
Cdd:COG2182 32 SSAAGAGGTLTVW--VDDDEAEALEEAAAAFEEE-PGIKVKVvEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 160 GLVLNLSQYLpqSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPY-PPNTTEQLVQIAESVNKTyHVWGIAY 238
Cdd:COG2182 109 GLLAPLDDDL--ADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAePPKTWDELIAAAKKLTAA-GKYGLAY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 239 GAGDeyGYRFAAWFAGFGGQIFATN-NGKIVPSLNSTAMVNALNFWYNLTYNLkvnyLAPSTGAGGAEGQLFVANQTAII 317
Cdd:COG2182 186 DAGD--AYYFYPFLAAFGGYLFGKDgDDPKDVGLNSPGAVAALEYLKDLIKDG----VLPADADYDAADALFAEGKAAMI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 318 FDGPWDLNAYLQALGPNLGAAPLPVVsQTGLRAAPFIGSTGFLIASPQASGAtqlqikAALIFVLYFTNYQADLRLWEVA 397
Cdd:COG2182 260 INGPWAAADLKKALGIDYGVAPLPTL-AGGKPAKPFVGVKGFGVSAYSKNKE------AAQEFAEYLTSPEAQKALFEAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 398 HDIPANLQAYNEAltQLKEgmlqptylNRIMEGILEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGMEQ 477
Cdd:COG2182 333 GRIPANKAAAEDA--EVKA--------DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQK 402
|
....*...
gi 502107763 478 AFIQALVQ 485
Cdd:COG2182 403 QIEAAIAQ 410
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
89-452 |
8.10e-48 |
|
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: 169.87 E-value: 8.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVTY-GVGVGTSQFETAAKAGQAPIVYRDTSDSGGALFAAGLVLNLSQ 167
Cdd:cd13657 1 TITIWHALTGAEEDALQQIIDEFEAKYPVPNVKVPFeKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 168 YLPQSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPYPPNTTEQLVQIAESV-NKTYHVWGIAYGAGDeyGY 246
Cdd:cd13657 81 YLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtDPAAGSYGLAYQVSD--AY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 247 RFAAWFAGFGGQIFATNNGKivPSLNSTAMVNAlnFWYNLTYNLKVnylAPSTGAGGAEGQLFVANQTAIIFDGPWDLNA 326
Cdd:cd13657 159 FVSAWIFGFGGYYFDDETDK--PGLDTPETIKG--IQFLKDFSWPY---MPSDPSYNTQTSLFNEGKAAMIINGPWFIGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 327 yLQALGPNLGAAPLPVVSQTGLrAAPFIGSTGFLIASPQASGAtqlqIKAALIFVLYFTNYQADLRLWEVAHDIPANLQA 406
Cdd:cd13657 232 -IKAAGIDLGVAPLPTVDGTNP-PRPYSGVEGIYVTKYAERKN----KEAALDFAKFFTTAEASKILADENGYVPAATNA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502107763 407 YNEALTQlkegmlqptyLNRIMEGILEQAQYGQQFPNIPQMAYYWN 452
Cdd:cd13657 306 YDDAEVA----------ADPVIAAFKAQAEHGVPMPNSPEMASVWG 341
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
89-478 |
1.77e-42 |
|
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: 155.91 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVTYgVGVGT---SQFETAAKAGQAPIVYRDTSDSGGALFAAGLVLNL 165
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVY-QGSYDdtlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 166 SQYLPQSVTSL--YVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKF-------VPYPPNTTEQLVQIAESV---NKTYHV 233
Cdd:cd14748 80 DDYIDKDGVDDddFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLfeeagldPEKPPKTWDELEEAAKKLkdkGGKTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 234 WGIAYGAGDEYGyRFAAWFAGFGGQIFATNNGKIVpsLNSTAMVNALNFWYNLTYNLKVNYLApstgAGGAEGQLFVANQ 313
Cdd:cd14748 160 YGFALPPGDGGW-TFQALLWQNGGDLLDEDGGKVT--FNSPEGVEALEFLVDLVGKDGVSPLN----DWGDAQDAFISGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 314 TAIIFDGPWDLNAYLQ-ALGPNLGAAPLPVVsqTGLRAAPFIGSTGFLIaspqASGATQlQIKAALIFVLYFTNYQADLR 392
Cdd:cd14748 233 VAMTINGTWSLAGIRDkGAGFEYGVAPLPAG--KGKKGATPAGGASLVI----PKGSSK-KKEAAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 393 LWEVAHDIPANLQAYNEALTQLKEgmlqptylNRIMEGILEQAQYGQ-QFPNIPQMAYYWNSFHQYASEFFANKINSTQA 471
Cdd:cd14748 306 WAKATGYLPVRKSAAEDPEEFLAE--------NPNYKVAVDQLDYAKpWGPPVPNGAEIRDELNEALEAALLGKKTPEEA 377
|
....*..
gi 502107763 472 AQGMEQA 478
Cdd:cd14748 378 LKEAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
81-416 |
2.59e-41 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 152.12 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 81 STAPSTPVTITVWnSYSTSENQAFNETLAQFEQAFPWIHVQVTYgvgVGTSQFE----TAAKAGQAPIVYRDTSDSGGAL 156
Cdd:COG1653 26 AAAAAGKVTLTVW-HTGGGEAAALEALIKEFEAEHPGIKVEVES---VPYDDYRtkllTALAAGNAPDVVQVDSGWLAEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 157 FAAGLVLNLSQYLPQS--VTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKF-----VPyPPNTTEQLVQIAESVNK 229
Cdd:COG1653 102 AAAGALVPLDDLLDDDglDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLfekagLD-PPKTWDELLAAAKKLKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 230 TYHVWGIAYGAGDeyGYRFAAWFAGFGGQIFaTNNGKIVpsLNSTAMVNALNFWYNLTYNLKVNYLAPSTGAGGAeGQLF 309
Cdd:COG1653 181 KDGVYGFALGGKD--GAAWLDLLLSAGGDLY-DEDGKPA--FDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDA-RAAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 310 VANQTAIIFDGPWDLNAYLQAL-GPNLGAAPLPVVsQTGLRAAPFIGSTGFLIASPQAsgatqlQIKAALIFVLYFTNYQ 388
Cdd:COG1653 255 ASGKAAMMINGSWALGALKDAApDFDVGVAPLPGG-PGGKKPASVLGGSGLAIPKGSK------NPEAAWKFLKFLTSPE 327
|
330 340
....*....|....*....|....*...
gi 502107763 389 ADLRlWEVAHDIPANLQAYNEALTQLKE 416
Cdd:COG1653 328 AQAK-WDALQAVLLGQKTPEEALDAAQA 354
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
89-478 |
1.94e-39 |
|
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: 147.55 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVT-YGVGVGTSQFETAAKAGQAP-IVYRDTSDsGGALFAAGLVLNLS 166
Cdd:cd13585 1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVpVPYDDYWTKLTTAAAAGTAPdVFYVDGPW-VPEFASNGALLDLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 167 QYLPQS-VTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK------FVPYPPNTTEQLVQIAESVNKTYH-VWGIAY 238
Cdd:cd13585 80 DYIEKDgLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDlfdkagPGPKPPWTWDELLEAAKKLTDKKGgQYGFAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 239 GAGDEYGYRFAAWFAGFGGQIFATNNGKIVpsLNSTAMVNALNFWYNLtYNLKVNYLAPSTGAGGAeGQLFVANQTAIIF 318
Cdd:cd13585 160 RGGSGGQTQWYPFLWSNGGDLLDEDDGKAT--LNSPEAVEALQFYVDL-YKDGVAPSSATTGGDEA-VDLFASGKVAMMI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 319 DGPWDLNAYL-QALGPNLGAAPLPVVsqTGLRAAPFIGSTGFLIASpqasgATQlQIKAALIFVLYFTNYQADLRLWEVA 397
Cdd:cd13585 236 DGPWALGTLKdSKVKFKWGVAPLPAG--PGGKRASVLGGWGLAISK-----NSK-HPEAAWKFIKFLTSKENQLKLGGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 398 HDIPANLQAYNEALTQLKEGMLQPTYlnrimegiLEQAQYGQQFPNIPQMAYYWNSFHQYASEFFANKINSTqAAQGMEQ 477
Cdd:cd13585 308 GPAALAAAAASAAAPDAKPALALAAA--------ADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKS-PEEALKE 378
|
.
gi 502107763 478 A 478
Cdd:cd13585 379 A 379
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
137-472 |
1.76e-35 |
|
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: 136.46 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 137 AKAGQAPIVYRDTSDSGGALFAAGLVLNLSqyLPQSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPYPPNT 216
Cdd:cd13658 48 GPAGKGPDVMVAPHDRIGSAVLQGLLSPIK--LSKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 217 TEQLVQIAESVN----KTYhvwGIAYGAGDEYgYRFAAwFAGFGGQIFATNNGKIVPS---LNSTAMVNALNF---WYNL 286
Cdd:cd13658 126 FDELEALAKDLTkekgKQY---GFLADATNFY-YSYGL-LAGNGGYIFKKNGSDLDINdigLNSPGAVKAVKFlkkWYTE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 287 TYnlkvnylAPSTGAGGAEGQLFVANQTAIIFDGPWDLNAYlQALGPNLGAAPLPVVSQtGLRAAPFIGSTGFLIasPQA 366
Cdd:cd13658 201 GY-------LPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEY-QEAGVNYGVAPLPTLPN-GKPMAPFLGVKGWYL--SAY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 367 SGatqlQIKAALIFVLYFTNYQADLRLWEVAHDIPANLQAYNEALTQlkegmlqptyLNRIMEGILEQAQYGQQFPNIPQ 446
Cdd:cd13658 270 SK----HKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIK----------NNPLTSAFAKQASRAVPMPNIPE 335
|
330 340
....*....|....*....|....*.
gi 502107763 447 MAYYWNSFHQyASEFFANKINSTQAA 472
Cdd:cd13658 336 MGAVWEPANN-ALFFILSGKKTPKQA 360
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
89-408 |
5.28e-29 |
|
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: 118.25 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVT-YGVGVGTSQFETAAKAGQAPIVYRdtSDSGG-ALFA-AGLVLNL 165
Cdd:cd14751 1 TITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAVrVPFDGLHNQIKTAAAGGQAPDVMR--ADIAWvPEFAkLGYLQPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 166 SQYLPQSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK-----FVPyPPNTTEQLVQIAESVNKTYHVWGiaYGA 240
Cdd:cd14751 79 DGTPAFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRlleeaGTE-VPKTMDELVAAAKAIKKKKGRYG--LYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 241 GDEYGYRFAAWFAGFGGQIfaTNNGKIVPSLNSTAMVNALNFWYNLtYNLKVNYLAPSTGAGGAEGQlFVANQTAIIFDG 320
Cdd:cd14751 156 SGDGPYWLLPFLWSFGGDL--TDEKKATGYLNSPESVRALETIVDL-YDEGAITPCASGGYPNMQDG-FKSGRYAMIVNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 321 PW----DLNAYLQALGPNLGAAPLPVvsqtglraapfiGSTGflIASPQasGATQLQI-------KAALIFVLYFTNYQA 389
Cdd:cd14751 232 PWayadILGGKEFKDPDNLGIAPVPA------------GPGG--SGSPV--GGEDLVIfkgsknkDAAWKFVKFMSSAEA 295
|
330
....*....|....*....
gi 502107763 390 DLRLWEVAHDIPANLQAYN 408
Cdd:cd14751 296 QALTAAKLGLLPTRTSAYE 314
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
89-475 |
9.54e-28 |
|
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: 114.36 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSystSENQAF-NETLAQFEQAFPWIHVQVTYGV-GVGTSQFETAAKAGQAPIVYRDTSDSGGALFAAGLVLNLS 166
Cdd:cd13655 1 TLTVWGP---QEDQEWlKEMVDAFKEKHPEWKITITIGVvGEADAKDEVLKDPSAAADVFAFANDQLGELVDAGAIYPLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 167 QYLPQSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKfvPYPPNTTEQLVQIAESVNKTYHVWGIAYGAgdeyGY 246
Cdd:cd13655 78 GSAVDKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKS--KLTEDDVKSLDTMLAKAPDAKGKVSFDLSN----SW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 247 RFAAWFAGFGGQIFATNNGKI-VPSLNSTAMVNALNFWYNLTYNLKVnylapSTGAGGAEGQLFVANQTAIIFDGPWDLN 325
Cdd:cd13655 152 YLYAFFFGAGCKLFGNNGGDTaGCDFNNEKGVAVTNYLVDLVANPKF-----VNDADGDAISGLKDGTLGAGVSGPWDAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 326 AYLQALGPNLGAAPLPVVS----QTGLRAapFIGSTGFLIaspqaSGATQLQiKAALIFVLYFTNYQADLRLWEVAHDIP 401
Cdd:cd13655 227 NLKKALGDNYAVAKLPTYTlggkDVQMKS--FAGYKAIGV-----NSNTKNP-EAAMALADYLTNEESQLTRFEKRGIGP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502107763 402 ANLQAY-NEALTQlkegmlqptylNRIMEGILEQAQYGQQ-FPNIPQMAYYWNSFHQYASEFFANKINSTQAAQGM 475
Cdd:cd13655 299 TNKEAAeSDAVKA-----------DPAAKALIAQSNEASVvQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQKL 363
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
89-479 |
1.34e-26 |
|
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: 111.32 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQ-AFNETLAQFEQAFPWIHV-QVTYGVGVGTSQFETAAKAGQAPIVYRdtSDSGG---ALFAAGLVL 163
Cdd:cd14749 1 TITYWQYFTGDTKKkYMDELIADFEKENPNIKVkVVVFPYDNYKTKLKTAVAAGEGPDVFN--LWPGGwlaEFVKAGLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 164 NLSQYL-PQSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK-FVPY----PPNTTEQLVQIAESVN-KTYHVWGI 236
Cdd:cd14749 79 PLTDYLdPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDlFEEAggvkPPKTWDELIEAAKKDKfKAKGQTGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 237 AYGAGDEYG---YRFAAWFAGfGGQIFATNNGKIvpSLNSTAMVNALNFWYNLTYNLKVNYLAPSTGAGGAeGQLFVANQ 313
Cdd:cd14749 159 GLLLGAQGGhwyFQYLVRQAG-GGPLSDDGSGKA--TFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDA-GQAFAQGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 314 TAIIFDGPWDLNAYLQALGP-NLGAAPLPVVSQTGLRAApfIGSTGFLIAsPQASGATQlqiKAALIFVLYFTNYQADLR 392
Cdd:cd14749 235 AAMNIGGSWDLGAIKAGEPGgKIGVFPFPTVGKGAQTST--IGGSDWAIA-ISANGKKK---EAAVKFLKYLTSPEVMKQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 393 LWEVahdipANLQAYNEALTqlKEGMLQPTYLNRIMEGILEQAQygqqfpNIPQMAYYWNSFHQYA----SEFFANKINS 468
Cdd:cd14749 309 YLED-----VGLLPAKEVVA--KDEDPDPVAILGPFADVLNAAG------STPFLDEYWPAAAQVHkdavQKLLTGKIDP 375
|
410
....*....|.
gi 502107763 469 TQAAQGMEQAF 479
Cdd:cd14749 376 EQVVKQAQSAA 386
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
89-446 |
7.17e-25 |
|
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: 106.24 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 89 TITVWNSYSTSENQAFNETLAQFEQAFPWIHVQVTY-GVGVGTSQFETAAKAGQAPIVYrDTSDSGGALFAA-GLVLNLS 166
Cdd:cd14747 1 TLTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVlPWGDAHTKITTAAASGDGPDVV-QLGNTWVAEFAAmGALEDLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 167 QYLPQSV-TSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK-----FVPYPPNTTEQLVQIAESVNKTY-HVWGIAYG 239
Cdd:cd14747 80 PYLEDLGgDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDllkkaGGDEAPKTWDELEAAAKKIKADGpDVSGFAIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 240 AGDEYGYRFAAWFAGFGGQIFATNNGKivPSLNSTAMVNALNFWYNLTYNLKVnyLAPSTGAGGAEGQLFVANQTAIIFD 319
Cdd:cd14747 160 GKNDVWHNALPFVWGAGGDLATKDKWK--ATLDSPEAVAGLEFYTSLYQKGLS--PKSTLENSADVEQAFANGKVAMIIS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 320 GPWDLNAyLQALGP----NLGAAPLPvvSQTGLRAAPFIGstGFLIASPQASGatqlQIKAALIFVLYFTNYQADLRLWE 395
Cdd:cd14747 236 GPWEIGA-IREAGPdlagKWGVAPLP--GGPGGGSPSFAG--GSNLAVFKGSK----NKDLAWKFIEFLSSPENQAAYAK 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502107763 396 VAHDIPANLQAYNEALTQLKEgmlqptylnrIMEGILEQAQYGQQFPNIPQ 446
Cdd:cd14747 307 ATGMLPANTSAWDDPSLANDP----------LLAVFAEQLKTGKATPATPE 347
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
100-478 |
4.85e-17 |
|
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: 83.11 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 100 ENQAFNETLAQFEQAFPWIHVQVTYGVGVGTSQFE-----TAAKAGQAPIVYRDTSDSGgaLFA-AGLVLNLSQYLPQSV 173
Cdd:cd14750 12 EGELLKKAIAAFEKKHPDIKVEIEELPASSDDQRQqlvtaLAAGSSAPDVLGLDVIWIP--EFAeAGWLLPLTEYLKEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 174 TSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKKFVPY----PPNTTEQLVQIAESVNKTYH-VWGIAYGAGDEYGY-- 246
Cdd:cd14750 90 DDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKygpePPKTWDELLEAAKKRKAGEPgIWGYVFQGKQYEGLvc 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 247 RFAAWFAGFGGQIFATNNGKIVpsLNSTAMVNALNFWYNLtYNLKVnylAPSTGAGGAE---GQLFVANQTAIIFDGPWD 323
Cdd:cd14750 170 NFLELLWSNGGDIFDDDSGKVT--VDSPEALEALQFLRDL-IGEGI---SPKGVLTYGEeeaRAAFQAGKAAFMRNWPYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 324 lNAYLQALGPNL----GAAPLPvvSQTGLRAAPFIGstGFLIASPQASGatqlQIKAALIFVLYFTNYQADLRLWEVAHD 399
Cdd:cd14750 244 -YALLQGPESAVagkvGVAPLP--AGPGGGSASTLG--GWNLAISANSK----HKEAAWEFVKFLTSPEVQKRRAINGGL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502107763 400 IPANLQAYNEAltQLKEGMlqPTYlnRIMEGILEQAQYGQQFPNIPQMAyywNSFHQYASEFFANKINSTQAAQGMEQA 478
Cdd:cd14750 315 PPTRRALYDDP--EVLEAY--PFL--PALLEALENAVPRPVTPKYPEVS---TAIQIALSAALSGQATPEEALKQAQEK 384
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
130-482 |
8.59e-17 |
|
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: 81.87 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 130 TSQFETAAKAGQAPIVYRDTSDSGGALFAAGLvlnLSQYLP-QSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK 208
Cdd:cd13656 40 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGL---LAEITPdKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 209 FVPYPPNTTEQLVQIAESV------------NKTYHVWGIaygagdeygyrfaawFAGFGGQIFATNNGKIVPS---LNS 273
Cdd:cd13656 117 LLPNPPKTWEEIPALDKELkakgksalmfnlQEPYFTWPL---------------IAADGGYAFKYENGKYDIKdvgVDN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 274 TAMVNALNFWYNLtynLKVNYLAPSTGAGGAEGQlFVANQTAIIFDGPWDLnAYLQALGPNLGAAPLPVVSqtGLRAAPF 353
Cdd:cd13656 182 AGAKAGLTFLVDL---IKNKHMNADTDYSIAEAA-FNKGETAMTINGPWAW-SNIDTSKVNYGVTVLPTFK--GQPSKPF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 354 IGSTGFLI--ASPQASGATQlqikaalifvlYFTNY-QADLRLWEVAHDIPAN---LQAYNEALTQlkegmlqptylNRI 427
Cdd:cd13656 255 VGVLSAGInaASPNKELAKE-----------FLENYlLTDEGLEAVNKDKPLGavaLKSYEEELAK-----------DPR 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502107763 428 MEGILEQAQYGQQFPNIPQMAYYWNSFHqyaseffANKINSTQAAQGMEQAFIQA 482
Cdd:cd13656 313 IAATMENAQKGEIMPNIPQMSAFWYAVR-------TAVINAASGRQTVDEALKDA 360
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
130-454 |
1.42e-13 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 72.35 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 130 TSQFETAAKAGQAPIVYRDTSDSGGALFAAGLvlnLSQYLP-QSVTSLYVPTAIKDWELNGSLYGLPDNVNYIVMFYNKK 208
Cdd:PRK09474 70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGL---LAEVTPsKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 209 FVPYPPNTTEQLVQIAESVNK------------TYHVWGIaygagdeygyrfaawFAGFGGQIFATNNGKIVPS---LNS 273
Cdd:PRK09474 147 LVPTPPKTWEEIPALDKELKAkgksaimwnlqePYFTWPL---------------IAADGGYAFKFENGGYDVKdvgVNN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 274 TAMVNALNFWYNLtynLKVNYLAPSTGAGGAEGQlFVANQTAIIFDGPWDLnAYLQALGPNLGAAPLPVVsqTGLRAAPF 353
Cdd:PRK09474 212 AGAKAGLQFLVDL---VKNKHMNADTDYSIAEAA-FNKGETAMTINGPWAW-SNIDKSGINYGVTVLPTF--NGKPSKPF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 354 IG--STGFLIASPQASGATQlqikaalifvlYFTNYQ-ADLRLWEVAHDIP---ANLQAYNEALTqlKEGMLQPTYLNri 427
Cdd:PRK09474 285 VGvlSAGINAASPNKELAKE-----------FLENYLlTDEGLETVNKDKPlgaVALKSFQEELA--KDPRIAATMDN-- 349
|
330 340
....*....|....*....|....*..
gi 502107763 428 megileqAQYGQQFPNIPQMAYYWNSF 454
Cdd:PRK09474 350 -------AQNGEIMPNIPQMSAFWYAM 369
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
109-410 |
1.65e-10 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 62.04 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 109 AQFEQAFPWIHVQVTYGVGVGTSQFETAAKAGQAP--IVYRDTSDSGGALFAAGLVLNLSQYlpqsVTSLYVPTAIKDWE 186
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPdlDVVWIAADQLATLAEAGLLADLSDV----DNLDDLPDALDAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 187 LNGSLYGLPDNVNY-IVMFYNKKFVP---YPPNTTEQLVQIAESV--NKTYHVWGIAYgagdeygYRFAAWFAGfggqif 260
Cdd:pfam13416 80 YDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLkgKTGLTDPATGW-------LLWALLADG------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 261 ATNNGKIVPSLNSTAmvnALNFWYNLTYNLKVnylaPSTGAGGAegQLFVANQTAIIFDGPWDLNAYLQAlGPNLGAAPL 340
Cdd:pfam13416 147 VDLTDDGKGVEALDE---ALAYLKKLKDNGKV----YNTGADAV--QLFANGEVAMTVNGTWAAAAAKKA-GKKLGAVVP 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 341 PvvsqtglrAAPFIGSTGFLIaspqASGATQLQIkAALIFVLYFTNYQADLRLWEVAHDIPANLQAYNEA 410
Cdd:pfam13416 217 K--------DGSFLGGKGLVV----PAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKSAALSD 273
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
97-358 |
4.20e-10 |
|
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: 60.89 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 97 STSENQAFNETLAQFEQAFPWIHVQVTYGV-GVGTSQFETAAKAGQAPI-VYRDTSDSGGALFAAGLVLNLSQYLPQsvt 174
Cdd:pfam01547 3 SLTEAAALQALVKEFEKEHPGIKVEVESVGsGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVAN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 175 slyvptaiKDWELNGSLYGLPDNVNYIVMFYNKKFVP----YPPNTTEQLVQIAESVN-KTYHVWGIAYG-AGDEYGYRF 248
Cdd:pfam01547 80 --------YLVLGVPKLYGVPLAAETLGLIYNKDLFKkaglDPPKTWDELLEAAKKLKeKGKSPGGAGGGdASGTLGYFT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 249 AAWFAGFGGQIFATNNGKivpsLNSTAMVNALNFWYNLTYNLKVNYLAPSTGAGGAEG----QLFVANQTAIIFDGPWDL 324
Cdd:pfam01547 152 LALLASLGGPLFDKDGGG----LDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGrealALFEQGKAAMGIVGPWAA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502107763 325 NAYLQA------------LGPNLGAAPLPVVSQTGLRAAPFIGSTG 358
Cdd:pfam01547 228 LAANKVklkvafaapapdPKGDVGYAPLPAGKGGKGGGYGLAIPKG 273
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
86-331 |
1.73e-06 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 50.40 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 86 TPVTITVWNSYSTSENQAF--NETLAQFEQAFPwIHVQVTYgvgVGTSQFE----TAAKAGQAP---IVYRDTSDSGgaL 156
Cdd:cd13580 1 EPVTITIVANLGGNPKPDPddNPYTKYLEEKTN-IDVKVKW---VPDSSYDeklnLALASGDLPdivVVNDPQLSIT--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 157 FAAGLVLNLSQYLPQSVTSLYVPTAIKDWE---LNGSLYGLP---DNVNYIVMFYNK----KFVPYPPNTTEQLVQIAE- 225
Cdd:cd13580 75 VKQGALWDLTDYLDKYYPNLKKIIEQEGWDsasVDGKIYGIPrkrPLIGRNGLWIRKdwldKLGLEVPKTLDELYEVAKa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502107763 226 ---------SVNKTYhvwGIAYGAGDEYG--YRFAAWFAGFGGQIFATNNGKIVPSLNSTAMVNALNF---WYN------ 285
Cdd:cd13580 155 ftekdpdgnGKKDTY---GLTDTKDLIGSgfTGLFGAFGAPPNNWWKDEDGKLVPGSIQPEMKEALKFlkkLYKeglidp 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502107763 286 --LTYNlkvnylapstgagGAEGQLFVANQTAIIFDGPWDLNAYLQAL 331
Cdd:cd13580 232 efAVND-------------GTKANEKFISGKAGIFVGNWWDPAWPQAS 266
|
|
| |
