|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
11-352 |
3.86e-52 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 179.08 E-value: 3.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 11 IFIAGLASALLLTACERGDDSAATATaaaEPVVLTALVWAPDWSEEMHRVADAFSLKHPEVRINLQFMIGNSVEENLKPR 90
Cdd:COG1653 5 ALALAAALALALAACGGGGSGAAAAA---GKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 91 AATDSLPDIVSVNaSPYTATLADQGLLADIGD-----TQAWGNMLEVLqREWTSPGGRRYGIPSGVATTLIYYNRDMFDR 165
Cdd:COG1653 82 LAAGNAPDVVQVD-SGWLAEFAAAGALVPLDDlldddGLDKDDFLPGA-LDAGTYDGKLYGVPFNTDTLGLYYNKDLFEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 166 AGITaPPADFESFLAAGAALR-KAGLVPLALPGGfpnmlgNGPFSYGFANQIAAKVPDwrariANGTLQLDNADGAAIFA 244
Cdd:COG1653 160 AGLD-PPKTWDELLAAAKKLKaKDGVYGFALGGK------DGAAWLDLLLSAGGDLYD-----EDGKPAFDSPEAVEALE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 245 RLRTLVEQKMVQTDCLRAGYDTTLRQFAEGRAAMTFQGSWAAGTLMNAR-GMRVGVFVPPWNDKGQPLKPVLGSeTGFAV 323
Cdd:COG1653 228 FLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGG-SGLAI 306
|
330 340 350
....*....|....*....|....*....|
gi 2526709387 324 AqrSGARQRQAAVQFLDFLYGP-GMPIWQA 352
Cdd:COG1653 307 P--KGSKNPEAAWKFLKFLTSPeAQAKWDA 334
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
6-433 |
1.66e-50 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 175.91 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 6 KRGLRIFIAGLASALLLTACERGDDSAATATAAAEPVVLTalVWAPDWSEE-MHRVADAFSlKHPEVRINLQFMIGNSVE 84
Cdd:COG2182 3 RRLLAALALALALALALAACGSGSSSSGSSSAAGAGGTLT--VWVDDDEAEaLEEAAAAFE-EEPGIKVKVVEVPWDDLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 85 ENLKPRAATDSLPDIVSVnASPYTATLADQGLLADIGDTQA-WGNMLEVLQREWTSpGGRRYGIPSGVATTLIYYNRDMF 163
Cdd:COG2182 80 EKLTTAAPAGKGPDVFVG-AHDWLGELAEAGLLAPLDDDLAdKDDFLPAALDAVTY-DGKLYGVPYAVETLALYYNKDLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 164 DragiTAPPADFESFLAAGAALRKAGLVPLALPGGfpNMLGNGPFSYGFANQIAAKVPDwrariANGTLQLDNADGAAIF 243
Cdd:COG2182 158 K----AEPPKTWDELIAAAKKLTAAGKYGLAYDAG--DAYYFYPFLAAFGGYLFGKDGD-----DPKDVGLNSPGAVAAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 244 ARLRTLVEQKMVQTDClraGYDTTLRQFAEGRAAMTFQGSWAAGTLMNARGMRVGVFVPPWNDKGQPLKPVLGSEtGFAV 323
Cdd:COG2182 227 EYLKDLIKDGVLPADA---DYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGKPAKPFVGVK-GFGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 324 AQRSgaRQRQAAVQFLDFLYGPGMPIWQAKRQNIPPFRVIAAD---VKGDPALFALVDQMTRDAAVSNAPGLyysvlpvN 400
Cdd:COG2182 303 SAYS--KNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEdaeVKADPLIAAFAEQAEYAVPMPNIPEM-------G 373
|
410 420 430
....*....|....*....|....*....|....
gi 2526709387 401 TI-DVLHPLLQSVLSGSQTPARAARLLQDSITEQ 433
Cdd:COG2182 374 AVwTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
57-428 |
1.78e-41 |
|
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: 151.38 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 57 MHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNASPYTATLADQGLLADIGDT----QAWGNMLEV 132
Cdd:cd14749 17 MDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDYldpnGVDKRFLPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 133 LQrEWTSPGGRRYGIPSGVATTLIYYNRDMFDRAGITAPPADFESFLAAGAALRKAGLV--PLALPGGFpnMLGNGPFSY 210
Cdd:cd14749 97 LA-DAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGqtGFGLLLGA--QGGHWYFQY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 211 gFANQIAakvPDWRARIANGTLQLDNADGAAIFARLRTLVEQKMVQTDCLRAGYDTTLRQFAEGRAAMTFQGSWAAGTLM 290
Cdd:cd14749 174 -LVRQAG---GGPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 291 NAR-GMRVGVFVPPWNDKGQPLKPVLGSetGFAVAQRSGARQRQAAVQFLDFLYGP-GMPIWQAKrQNIPPFRVIAAdVK 368
Cdd:cd14749 250 AGEpGGKIGVFPFPTVGKGAQTSTIGGS--DWAIAISANGKKKEAAVKFLKYLTSPeVMKQYLED-VGLLPAKEVVA-KD 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 369 GDPALFALVDQMTrDAAVSNAPGLYYSVLPVNTIDVLHPLLQSVLSGSQTPARAARLLQD 428
Cdd:cd14749 326 EDPDPVAILGPFA-DVLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQS 384
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
48-430 |
1.78e-34 |
|
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: 132.14 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 48 VWAPDWSEE---MHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNaSPYTATLADQGLLADIGD-- 122
Cdd:cd13585 4 FWDWGQPAEtaaLKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVD-GPWVPEFASNGALLDLDDyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 123 --TQAWGNMLEVLQrEWTSPGGRRYGIPSGVATTLIYYNRDMFDRAG-ITAPPADFESFLAAGAALRKAGLV--PLALPG 197
Cdd:cd13585 83 ekDGLDDDFPPGLL-DAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpGPKPPWTWDELLEAAKKLTDKKGGqyGFALRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 198 GFPNMLGNGPFSYGFANQIAAKvpdwrariANGTLQLDNADGAAIFARLRTLVEQKMVQTDcLRAGYDTTLRQFAEGRAA 277
Cdd:cd13585 162 GSGGQTQWYPFLWSNGGDLLDE--------DDGKATLNSPEAVEALQFYVDLYKDGVAPSS-ATTGGDEAVDLFASGKVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 278 MTFQGSWAAGTLMNARGM-RVGVFVPPWNDKGQPlKPVLGSeTGFAVAqrSGARQRQAAVQFLDFLYGP-GMPIWQAKRQ 355
Cdd:cd13585 233 MMIDGPWALGTLKDSKVKfKWGVAPLPAGPGGKR-ASVLGG-WGLAIS--KNSKHPEAAWKFIKFLTSKeNQLKLGGAAG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526709387 356 NIPPFRVIAADVKGDPALFALVDQMTRDAAVSNAPGLYYSVLPVNTIdvLHPLLQSVLSGS--QTPARAARLLQDSI 430
Cdd:cd13585 309 PAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPI--LSEALQEALLGAlgKSPEEALKEAAKEI 383
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
49-430 |
4.74e-33 |
|
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: 128.18 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 49 WAPDWSEEMHRVADAFSLKHPEVRINLQFMIGNSVEEN-LKPRAATDSLPDIVSVNASpYTATLADQGLLADI-----GD 122
Cdd:cd14748 8 MSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTkLLAALAAGTAPDVAQVDAS-WVAQLADSGALEPLddyidKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 123 TQAWGNMLEVLQREWTSpGGRRYGIPSGVATTLIYYNRDMFDRAG--ITAPPADFESFLAAGAALRKAGLVPLALPGGFP 200
Cdd:cd14748 87 GVDDDDFYPAALDAGTY-DGKLYGLPFDTSTPVLYYNKDLFEEAGldPEKPPKTWDELEEAAKKLKDKGGKTGRYGFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 201 NMLGNGPFsYGFANQiaakvpdwrariANGTLqLDNADGAAIFAR---------LRTLVEQKMVQTDclrAGYDTTLRQF 271
Cdd:cd14748 166 PGDGGWTF-QALLWQ------------NGGDL-LDEDGGKVTFNSpegvealefLVDLVGKDGVSPL---NDWGDAQDAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 272 AEGRAAMTFQGSWAAGTLM-NARGMRVGVFVPPWNDKGQPlKPVLGSeTGFAVAqRSGARQRQAAVQFLDFLYGP-GMPI 349
Cdd:cd14748 229 ISGKVAMTINGTWSLAGIRdKGAGFEYGVAPLPAGKGKKG-ATPAGG-ASLVIP-KGSSKKKEAAWEFIKFLTSPeNQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 350 WQAKRQNIPPFRVIAAD----VKGDPALFALVDQMtrDAAVSNAPGLYYSvlpVNTIDVLHPLLQSVLSGSQTPARAARL 425
Cdd:cd14748 306 WAKATGYLPVRKSAAEDpeefLAENPNYKVAVDQL--DYAKPWGPPVPNG---AEIRDELNEALEAALLGKKTPEEALKE 380
|
....*
gi 2526709387 426 LQDSI 430
Cdd:cd14748 381 AQEKI 385
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
48-391 |
1.60e-26 |
|
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: 110.10 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 48 VWA---PDWSEEMHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNASpYTATLADQGLLADIGD-T 123
Cdd:cd14747 4 VWAmgnSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNT-WVAEFAAMGALEDLTPyL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 124 QAWGNMLEVLQREWTSP--GGRRYGIPSGVATTLIYYNRDMFDRAGITAPPADFESFLAAGAALRKAG--LVPLALPGGF 199
Cdd:cd14747 83 EDLGGDKDLFPGLVDTGtvDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGpdVSGFAIPGKN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 200 PNMLGNGPFSYGFANQIAAKvPDWRAriangtlQLDNADGAAIFARLRTLVEQKMVQTDCLRAGYDTtlRQ-FAEGRAAM 278
Cdd:cd14747 163 DVWHNALPFVWGAGGDLATK-DKWKA-------TLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADV--EQaFANGKVAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 279 TFQGSWAAGTLMNARGM---RVGVFVPPwndkGQPLKPVLGSETGFAVAQRSGARQRQAAVQFLDFLYGP-GMPIWQAKR 354
Cdd:cd14747 233 IISGPWEIGAIREAGPDlagKWGVAPLP----GGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPeNQAAYAKAT 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 2526709387 355 QNIPPFRVIAADVKG--DPALFALVDQMTRDAAVSNAPG 391
Cdd:cd14747 309 GMLPANTSAWDDPSLanDPLLAVFAEQLKTGKATPATPE 347
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
57-346 |
5.66e-23 |
|
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: 98.26 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 57 MHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNASPYTATLADQGLLADIGDtqawgnmleVLQRE 136
Cdd:pfam01547 10 LQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDD---------YVANY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 137 WTSPGGRRYGIPSGVATTLIYYNRDMFDRAGITaPPADFESFLAAGAALRKAGLVPLALPGGFpNMLGNGPFSYGFANQI 216
Cdd:pfam01547 81 LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD-PPKTWDELLEAAKKLKEKGKSPGGAGGGD-ASGTLGYFTLALLASL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 217 AAKVPDWRARIANGTLQLDnADGAAIFARLRTLVEQKMVQTDCLRAGYDTTLRQFAEGRAAMTFQGSWAAGTLMNARGMR 296
Cdd:pfam01547 159 GGPLFDKDGGGLDNPEAVD-AITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2526709387 297 VGVFVPPWNDKGQPLKPVLGSETGFAVAQ----RSGARQRQAAVQFLDFLYGPG 346
Cdd:pfam01547 238 AFAAPAPDPKGDVGYAPLPAGKGGKGGGYglaiPKGSKNKEAAKKFLDFLTSPE 291
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
57-430 |
1.86e-22 |
|
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270454 [Multi-domain] Cd Length: 376 Bit Score: 98.22 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 57 MHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNaSPYTATLADQGLLADIGDTQAWGNMLEVLQR- 135
Cdd:cd14751 16 YEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRAD-IAWVPEFAKLGYLQPLDGTPAFDDIVDYLPGp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 136 -EWTSPGGRRYGIPSGVATTLIYYNRDMFDRAGiTAPPADFESFLA-AGAALRKAGLVPLALPGGFP-NMLgngPFSYGF 212
Cdd:cd14751 95 mETNRYNGHYYGVPQVTNTLALFYNKRLLEEAG-TEVPKTMDELVAaAKAIKKKKGRYGLYISGDGPyWLL---PFLWSF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 213 anqiAAKVPDWRARiangTLQLDNADGAAIFARLRTLVEQKMVQTdCLRAGYDTTLRQFAEGRAAMTFQGSWAAGTLMN- 291
Cdd:cd14751 171 ----GGDLTDEKKA----TGYLNSPESVRALETIVDLYDEGAITP-CASGGYPNMQDGFKSGRYAMIVNGPWAYADILGg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 292 ---ARGMRVGVFVPPWNDKGQPlkPVLGSETgfaVAQRSGARQRQAAVQFLDFLYGPGMPIWQAKRQNIPPFRVIAAD-- 366
Cdd:cd14751 242 kefKDPDNLGIAPVPAGPGGSG--SPVGGED---LVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYEsp 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526709387 367 -VKGDPALFALVDQMtrDAAVSNAPglyysVLPVNTIDV-LHPLLQSVLSGSQTPARAARLLQDSI 430
Cdd:cd14751 317 eVANNPMVAAFKPAL--ETAVPRPP-----IPEWGELFEpLTLAFAKVLRGEKSPREALDEAAKQW 375
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
60-427 |
4.43e-22 |
|
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: 97.10 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 60 VADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIV---SVNASPYTATladqGLLADIGDTQAWGNMLEVLQRE 136
Cdd:cd13522 19 LIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVfgpSDSLGPFAAA----GLLAPLDEYVSKSGKYAPNTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 137 WTSPGGRRYGIPSGVATTLIYYNRDMFdragITAPPADFESFLAAGAALRKAGLVPLALPGGFPnmLGNGPFSYGFANQI 216
Cdd:cd13522 95 AMKLNGKLYGVPVSVGAHLMYYNKKLV----PKNPPKTWQELIALAQGLKAKNVWGLVYNQNEP--YFFAAWIGGFGGQV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 217 aakvpdWRARIANGTLQLDNADGAAIFARLRTLVEQ-KMVQTDClraGYDTTLRQFAEGRAAMTFQGSWAAGTLMNARGM 295
Cdd:cd13522 169 ------FKANNGKNNPTLDTPGAVEALQFLVDLKSKyKIMPPET---DYSIADALFKAGKAAMIINGPWDLGDYRQALKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 296 RVGVFVPPWNDKGQPLKPVLGSeTGFAVAQRSgaRQRQAAVQFLDFLYGPGMPIWQAKRQNIPPFRVIAAD---VKGDPA 372
Cdd:cd13522 240 NLGVAPLPTFSGTKHAAPFVGG-KGFGINKES--QNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYEspaVQNKPA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526709387 373 LFALVDQMTRDAAVSNAPGL-YYSvlpvntiDVLHPLLQSVLSGSQTPARAARLLQ 427
Cdd:cd13522 317 QKASAEQAAYGVPMPNIPEMrAVW-------DAFRIAVNSVLAGKVTPEAAAKDAQ 365
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
55-430 |
1.01e-20 |
|
The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270304 [Multi-domain] Cd Length: 367 Bit Score: 93.13 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 55 EEMHRVADAFSLKHPeVRINLQFMIGNSVEENLKPRAATDSLPDIVsvnASPY--TATLADQGLLADIGDTQAwgNMLEV 132
Cdd:cd13586 13 EYLKELAEEFEKKYG-IKVEVVYVDSGDTREKFITAGPAGKGPDVF---FGPHdwLGELAAAGLLAPIPEYLA--VKIKN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 133 LQREW--TSPGGRRYGIPSGVATTLIYYNRDMfdragITAPPADFESFLAAGAA--LRKAGLVPLALPGGFPNMlgNGPF 208
Cdd:cd13586 87 LPVALaaVTYNGKLYGVPVSVETIALFYNKDL-----VPEPPKTWEELIALAKKfnDKAGGKYGFAYDQTNPYF--SYPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 209 SYGFANQIAAKVPDWRARIAngtlqLDNADGAAIFARLRTLVE--QKMVQTDclraGYDTTLRQFAEGRAAMTFQGSWAA 286
Cdd:cd13586 160 LAAFGGYVFGENGGDPTDIG-----LNNEGAVKGLKFIKDLKKkyKVLPPDL----DYDIADALFKEGKAAMIINGPWDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 287 GTlMNARGMRVGVFVPPWNDKGQPLKPVLGSeTGFAVAqrSGARQRQAAVQFLDFLYGPGMPIWQAKRQNIPPFRVIA-- 364
Cdd:cd13586 231 AD-YKDAGINFGVAPLPTLPGGKQAAPFVGV-QGAFVS--AYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDAln 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526709387 365 -ADVKGDPALFALVDQMTRDAAVSNAPglyysvlPVNTI-DVLHPLLQSVLSGSQTPARAARLLQDSI 430
Cdd:cd13586 307 dAAVKNDPLVKAFAEQAQYGVPMPNIP-------EMAAVwDAMGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
60-373 |
2.55e-20 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 90.54 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 60 VADAFSLKHPeVRINLQFMIGNSVEENLKPRAATDSLPDIVSVN-ASPYTATLADQGLLADIGDTQAWGNMLEVLqrEWT 138
Cdd:pfam13416 2 LAKAFEKKTG-VTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWiAADQLATLAEAGLLADLSDVDNLDDLPDAL--DAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 139 SPGGRRYGIPSGV-ATTLIYYNRDMFDRAGitAPPADFESFLAAGAALrkaglvplalPGGFpnMLGNGPFSYGFANQIA 217
Cdd:pfam13416 79 GYDGKLYGVPYAAsTPTVLYYNKDLLKKAG--EDPKTWDELLAAAAKL----------KGKT--GLTDPATGWLLWALLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 218 AKVPdwrariANGTLQLdNADGAAIFARLRTLVEQKMVqtdclRAGYDTTLRQFAEGRAAMTFQGSWAAGTLMNArGMRV 297
Cdd:pfam13416 145 DGVD------LTDDGKG-VEALDEALAYLKKLKDNGKV-----YNTGADAVQLFANGEVAMTVNGTWAAAAAKKA-GKKL 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526709387 298 GVFVPpwndkgqPLKPVLGSEtGFAVAQRSGARqRQAAVQFLDFLYGP-GMPIWQAKRQNIPPFRVIAAD--VKGDPAL 373
Cdd:pfam13416 212 GAVVP-------KDGSFLGGK-GLVVPAGAKDP-RLAALDFIKFLTSPeNQAALAEDTGYIPANKSAALSdeVKADPAL 281
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
46-430 |
2.34e-15 |
|
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270453 [Multi-domain] Cd Length: 385 Bit Score: 77.33 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 46 ALVWA----PDWSEEMHRVADAFSLKHPEVRINLQFMIGNSVEENLK---PRAATDSLPDIVSVNaSPYTATLADQGLLA 118
Cdd:cd14750 1 TITFAagsdGQEGELLKKAIAAFEKKHPDIKVEIEELPASSDDQRQQlvtALAAGSSAPDVLGLD-VIWIPEFAEAGWLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 119 DI-GDTQAWGNMLEVLQ-REWTSPGGRRYGIPSGVATTLIYYNRDMFDRAGITaPPADFESFLAAGAALRKA--GLVPLA 194
Cdd:cd14750 80 PLtEYLKEEEDDDFLPAtVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPE-PPKTWDELLEAAKKRKAGepGIWGYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 195 LPGGfpnmLGNG------PFSYGFANQIAAKvpdwrariANGTLQLDNADGAAIFARLRTLVEQKMVQTDCLRAGYDTTL 268
Cdd:cd14750 159 FQGK----QYEGlvcnflELLWSNGGDIFDD--------DSGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 269 RQFAEGRAAmtFQGSW-AAGTLMNARGMRV-GVF----VPPWndKGQPLKPVLGsetGFAVAQRSGARQRQAAVQFLDFL 342
Cdd:cd14750 227 AAFQAGKAA--FMRNWpYAYALLQGPESAVaGKVgvapLPAG--PGGGSASTLG---GWNLAISANSKHKEAAWEFVKFL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 343 YGPGMPIWQAKRQNIPPFRVIAAD----VKGDPALFALVDQMTRDAAVSNAPglYYSvlpvNTIDVLHPLLQSVLSGSQT 418
Cdd:cd14750 300 TSPEVQKRRAINGGLPPTRRALYDdpevLEAYPFLPALLEALENAVPRPVTP--KYP----EVSTAIQIALSAALSGQAT 373
|
410
....*....|..
gi 2526709387 419 PARAARLLQDSI 430
Cdd:cd14750 374 PEEALKQAQEKL 385
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
48-433 |
2.80e-14 |
|
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: 74.06 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 48 VWA-PDWSEE-MHRVADAFSlKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVnasPY--TATLADQGLLADIGDT 123
Cdd:cd13658 4 VWVdEDKKMAfIKKIAKQYT-KKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVA---PHdrIGSAVLQGLLSPIKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 124 QAWGNMLEVLQREWTSPGGRRYGIPSGVATTLIYYNRDMFDRAgitapPADFESFLAAGAALRKaglvPLALPGGFPNML 203
Cdd:cd13658 80 KDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA-----PKTFDELEALAKDLTK----EKGKQYGFLADA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 204 GNGPFSYGFanqIAA------KVPDWRARIANGTLQLDNADGAAIFArlrtlveQKMVQTDCLRAG--YDTTLRQFAEGR 275
Cdd:cd13658 151 TNFYYSYGL---LAGnggyifKKNGSDLDINDIGLNSPGAVKAVKFL-------KKWYTEGYLPKGmtGDVIQGLFKEGK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 276 AAMTFQGSWAAGTLMNArGMRVGVFVPPWNDKGQPLKPVLGSEtGFAVAQRSgaRQRQAAVQFLDFLYGPGmpiWQAKR- 354
Cdd:cd13658 221 AAAVIDGPWAIQEYQEA-GVNYGVAPLPTLPNGKPMAPFLGVK-GWYLSAYS--KHKEWAQKFMEFLTSKE---NLKKRy 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 355 ---QNIPPfRVIA---ADVKGDPALFALVDQMTRDAAVSNAPGLYYSVLPVNTidvlhpLLQSVLSGSQTPARAARLLQD 428
Cdd:cd13658 294 detNEIPP-RKDVrsdPEIKNNPLTSAFAKQASRAVPMPNIPEMGAVWEPANN------ALFFILSGKKTPKQALNDAVN 366
|
....*
gi 2526709387 429 SITEQ 433
Cdd:cd13658 367 DIKEN 371
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
48-430 |
7.99e-14 |
|
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: 72.41 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 48 VWApDWSEE----MHRVADAFSLKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVsVNASPYTATLADQGLLADIGD- 122
Cdd:cd13657 4 IWH-ALTGAeedaLQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLF-IWAHDWIGQFAEAGLLVPISDy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 123 -TQAWGNMLEVLQREWTSPGGRRYGIPSGVATTLIYYNRDMFDragitAPPADFESFLAAGAALRKAGlvplalPG--GF 199
Cdd:cd13657 82 lSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVD-----QPPETTDELLAIMKDHTDPA------AGsyGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 200 PNMLGNGPFSYGFANQIAAKVPDwrariaNGTLQ--LDNADGAAIFARLRTLVEQKMVQTDclraGYDTTLRQFAEGRAA 277
Cdd:cd13657 151 AYQVSDAYFVSAWIFGFGGYYFD------DETDKpgLDTPETIKGIQFLKDFSWPYMPSDP----SYNTQTSLFNEGKAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 278 MTFQGSWAAGTLmNARGMRVGVFVPPWNDKGQPLKPVLGSEtGFAVAQRSGARQRQAAVQFLDFLYGPGMPIWQAKRQNI 357
Cdd:cd13657 221 MIINGPWFIGGI-KAAGIDLGVAPLPTVDGTNPPRPYSGVE-GIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGY 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526709387 358 PPFRVIA---ADVKGDPALFALVDQMTRDAAVSNAPGLYYSVLPVNTIdvlhplLQSVLSGSQTPARAARLLQDSI 430
Cdd:cd13657 299 VPAATNAyddAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLA------LAAVYQGGQDPQEALAAAQQEI 368
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
92-171 |
5.31e-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: 55.03 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 92 ATDSLPDIVSVNASPYTATLADQGLLADIGD--TQAWGNMLEVLQREW---TSPGGRRYGIPSGVA---TTLIYYNRDMF 163
Cdd:cd13580 55 ASGDLPDIVVVNDPQLSITLVKQGALWDLTDylDKYYPNLKKIIEQEGwdsASVDGKIYGIPRKRPligRNGLWIRKDWL 134
|
....*...
gi 2526709387 164 DRAGITAP 171
Cdd:cd13580 135 DKLGLEVP 142
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
60-345 |
9.39e-08 |
|
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 53.00 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 60 VADAFSLKHPevrINLQFMIGNSVEENLKPRAATDSLP-DIVSVNaSPYTATLADQGLLADIgDTQAWGNMLEVLQREwt 138
Cdd:cd13589 19 VIEPFEKETG---IKVVYDTGTSADRLAKLQAQAGNPQwDVVDLD-DGDAARAIAEGLLEPL-DYSKIPNAAKDKAPA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 139 sPGGRRYGIPSGVATTLIYYNRDMFDRAGITAPPADFEsflaagaalrkaglvplaLPGGFPnmLGNGPFSYGFANQIAA 218
Cdd:cd13589 92 -ALKTGYGVGYTLYSTGIAYNTDKFKEPPTSWWLADFW------------------DVGKFP--GPRILNTSGLALLEAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 219 kvpdwrARIANGTLQLDNADGAaiFARLRTLVEQkmVQTdclragYDTTLRQFAEgraaMTFQGSWAAGTLMNARgmrvg 298
Cdd:cd13589 151 ------LLADGVDPYPLDVDRA--FAKLKELKPN--VVT------WWTSGAQLAQ----LLQSGEVDMAPAWNGR----- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2526709387 299 vfVPPWNDKGQPLKPVLGSETGFAVAQR----SGARQRQAAVQFLDFLYGP 345
Cdd:cd13589 206 --AQALIDAGAPVAFVWPKEGAILGPDTlaivKGAPNKELAMKFINFALSP 254
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
10-382 |
1.33e-07 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 53.38 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 10 RIFIAGLASALLLTACergddsaATATAAAEPVVLTALVWAPDWSEEmhrVADAFSLKHpEVRINLQFMIGNSV-EENLK 88
Cdd:COG0687 4 RSLLGLAAAALAAALA-------GGAPAAAAEGTLNVYNWGGYIDPD---VLEPFEKET-GIKVVYDTYDSNEEmLAKLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 89 praATDSLPDIVSVNaSPYTATLADQGLLADIGDTQ--AWGNMLEVLQREWTSPGgRRYGIPSGVATTLIYYNRDMFDra 166
Cdd:COG0687 73 ---AGGSGYDVVVPS-DYFVARLIKAGLLQPLDKSKlpNLANLDPRFKDPPFDPG-NVYGVPYTWGTTGIAYNTDKVK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 167 gitAPPADFESF----LAAGAALRKAG--LVPLALpggfpNMLGNGPFSygfanqiaakvpdwrariangtlqLDNADGA 240
Cdd:COG0687 146 ---EPPTSWADLwdpeYKGKVALLDDPreVLGAAL-----LYLGYDPNS------------------------TDPADLD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 241 AIFARLRTLVEQkmVQTdclragYDTTLRQ----FAEGRAAMTFQGSWAAGTLMnARGMRVGVFVPP-----WNDkgqpl 311
Cdd:COG0687 194 AAFELLIELKPN--VRA------FWSDGAEyiqlLASGEVDLAVGWSGDALALR-AEGPPIAYVIPKegallWFD----- 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526709387 312 kpvlgsetGFAVAqrSGARQRQAAVQFLDFLYGPGMPIWQAKRQNIPP-----FRVIAADVKGDPALFALVDQMTR 382
Cdd:COG0687 260 --------NMAIP--KGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPpnkaaRELLPPELAANPAIYPPEEVLDK 325
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
82-340 |
3.33e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 48.85 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 82 SVEENLKPRAATDSLPDIVsVNASPYTATLADQGLLADIGDTQAWGNMLEVLQREWTSPGGRRYGIPSGV-ATTLIYyNR 160
Cdd:PRK09474 68 KLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVeALSLIY-NK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 161 DMfdragITAPPADFESFLAAGAALRKAG----LVPLALPG-GFPNMLGNGPFSYGFANQiAAKVPDwrariangtLQLD 235
Cdd:PRK09474 146 DL-----VPTPPKTWEEIPALDKELKAKGksaiMWNLQEPYfTWPLIAADGGYAFKFENG-GYDVKD---------VGVN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 236 NADGAAIFARLRTLVEQKMVQTDclrAGYDTTLRQFAEGRAAMTFQGSWAAGTLMNArGMRVGVFVPPwNDKGQPLKPVL 315
Cdd:PRK09474 211 NAGAKAGLQFLVDLVKNKHMNAD---TDYSIAEAAFNKGETAMTINGPWAWSNIDKS-GINYGVTVLP-TFNGKPSKPFV 285
|
250 260
....*....|....*....|....*
gi 2526709387 316 GSetgFAVAQRSGARQRQAAVQFLD 340
Cdd:PRK09474 286 GV---LSAGINAASPNKELAKEFLE 307
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
92-345 |
4.57e-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: 270301 [Multi-domain] Cd Length: 478 Bit Score: 48.89 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 92 ATDSLPDIVSVNASPYTATLADQGLLADIGD-TQAWGNMLEVLQrEWT---------SPGGRRYGIP-----SGVATTLi 156
Cdd:cd13583 53 ASGDAPDIIPVLYPGEENEFVASGALLPISDyLDYMPNYKKYVE-KWGlgkelatgrQSDGKYYSLPglhedPGVQYSF- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 157 YYNRDMFDRAGITaPPADFESFLAAGAALRKAG--LVPLALPGGFPNMLGNGPFSYGfANQIAAKVP---DWRA-RIANG 230
Cdd:cd13583 131 LYRKDIFEKAGIK-IPTTWDEFYAALKKLKEKYpdSYPYSDRWNSNALLLIAAPAFG-TTAGWGFSNytyDPDTdKFVYG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 231 TLQlDNADGAAIFarLRTLVEQKMVQTDCLRAGYDTTLRQFAEGRAAMTFQGSWAAGTLMNARG---------MRVGVFV 301
Cdd:cd13583 209 ATT-DEYKDMLQY--FNKLYAEGLLDPESFTQTDDQAKAKFLNGKSFVITTNPQTVDELQRNLRaadggnyevVSITPPA 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2526709387 302 PPwndKGQPLKPVLGsETGFAVAQR-SGARQRQAAVQFLDFLYGP 345
Cdd:cd13583 286 GP---AGKAINGSRL-ENGFMISSKaKDSKNFEALLQFLDWLYSD 326
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
84-316 |
1.00e-05 |
|
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: 47.59 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 84 EENLKPRAATDSLPDIVsVNASPYTATLADQGLLADIGDTQAWGNMLEVLQREWTSPGGRRYGIPSGVATTLIYYNRDMf 163
Cdd:cd13656 40 EEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 164 dragITAPPADFESFLAAGAALRKAG----LVPLALPG-GFPNMLGNGPFSYGFANQiAAKVPDwrariangtLQLDNAD 238
Cdd:cd13656 118 ----LPNPPKTWEEIPALDKELKAKGksalMFNLQEPYfTWPLIAADGGYAFKYENG-KYDIKD---------VGVDNAG 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526709387 239 GAAIFARLRTLVEQKMVQTDclrAGYDTTLRQFAEGRAAMTFQGSWAAGTLmNARGMRVGVFVPPwNDKGQPLKPVLG 316
Cdd:cd13656 184 AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAMTINGPWAWSNI-DTSKVNYGVTVLP-TFKGQPSKPFVG 256
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
60-376 |
2.08e-05 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 46.08 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 60 VADAFSLKHpEVRINLQFMIGNSVEENLKpRAATDSLPDIVSVNASPYTATLADQGLLADIgDTQAWGNMLEvlqrEWTS 139
Cdd:COG1840 1 LLEAFEKKT-GIKVNVVRGGSGELLARLK-AEGGNPPADVVWSGDADALEQLANEGLLQPY-KSPELDAIPA----EFRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 140 PGGRRYGIpsGVATTLIYYNRDMFDRAGItapPADFESFLAagAALRkaGLVPLALPggfpnmlGNGPFSYGFANQIaak 219
Cdd:COG1840 74 PDGYWFGF--SVRARVIVYNTDLLKELGV---PKSWEDLLD--PEYK--GKIAMADP-------SSSGTGYLLVAAL--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 220 vpdwrariangtLQLDNADGAaiFARLRTLVEQKMVQTDCLRAgydtTLRQFAEGRAAMTFQGSWAAGTLMnARGMRVGV 299
Cdd:COG1840 135 ------------LQAFGEEKG--WEWLKGLAANGARVTGSSSA----VAKAVASGEVAIGIVNSYYALRAK-AKGAPVEV 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526709387 300 FVPpwNDKgqplkpVLGSETGFAVAQrsGARQRQAAVQFLDFLYGPGMPIWQAKRQNIPPfrvIAADVKGDPALFAL 376
Cdd:COG1840 196 VFP--EDG------TLVNPSGAAILK--GAPNPEAAKLFIDFLLSDEGQELLAEEGYEYP---VRPDVEPPEGLPPL 259
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
98-345 |
1.99e-04 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270308 [Multi-domain] Cd Length: 315 Bit Score: 42.99 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 98 DIVSVNASpYTATLADQGLLA--DIGDTQAWGNMLEVLQREWTSPGgRRYGIPSGVATTLIYYNRDMFDRagitaPPADF 175
Cdd:cd13590 51 DLVVPSDY-MVERLIKQGLLEplDHSKLPNLKNLDPQFLNPPYDPG-NRYSVPYQWGTTGIAYNKDKVKE-----PPTSW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 176 ESFLAAgAALRKaglvPLALPGGFPNMLGNGPFSYGFanqiaaKVPDWrariangtlqlDNADGAAIFARLRTLVEQkmv 255
Cdd:cd13590 124 DLDLWD-PALKG----RIAMLDDAREVLGAALLALGY------SPNTT-----------DPAELAAAAELLIKQKPN--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 256 qtdcLRA-GYDTTLRQFAEGRAAMTFQGSWAAGTLMNARGmRVGVFVPP-----WNDkgqplkpvlgsetGFAVAqrSGA 329
Cdd:cd13590 179 ----VRAfDSDSYVQDLASGEIWLAQAWSGDALQANRENP-NLKFVIPKeggllWVD-------------NMAIP--KGA 238
|
250
....*....|....*.
gi 2526709387 330 RQRQAAVQFLDFLYGP 345
Cdd:cd13590 239 PNPELAHAFINFLLDP 254
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
41-345 |
3.79e-04 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 42.83 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 41 PVVLTALV--WAPDWSEEMHRVADAFSlKHPEVRINLQFMIGNSVEENLKPRAATDSLPDIVSVNASPYTATLA-DQGLL 117
Cdd:cd13521 1 PLTLSVLMafNDNWVDDENWPVAKEIE-KLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIAYgMEGAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 118 ADIGDTQAWGNMLEVL-------QREWTSPGGRRYGIPS----GVATTLIYYNRDMFDRAGITAPPA--DFESFLAAGAA 184
Cdd:cd13521 80 LPLSKYIDQYPNLKAFfkqhpdvLRASTASDGKIYLIPYeppkDVPNQGYFIRKDWLDKLNLKTPKTldELYNVLKAFKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 185 -----LRKAGLVPLALPGGfpnmlGNGPF----SYGFANQIAAKVPDWRarIANGTLQLDNADGA--AIFARLRTLVEQK 253
Cdd:cd13521 160 kdpngNGKADEIPFIDRDP-----LYGAFrlinSWGARSAGGSTDSDWY--EDNGKFKHPFASEEykDGMKYMNKLYTEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 254 MVQTDCLRAGYDTTLRQFAEGRA-AMTFQGSWAAGTLMNARGMRVGVF-----VPPWNDKGQPL--KPVLGSETGFAVAq 325
Cdd:cd13521 233 LIDKESFTQKDDQAEQKFSNGKLgGFTHNWFASDNLFTAQLGKEKPMYillpiAPAGNVKGRREedSPGYTGPDGVAIS- 311
|
330 340
....*....|....*....|
gi 2526709387 326 rSGARQRQAAVQFLDFLYGP 345
Cdd:cd13521 312 -KKAKNPVAALKFFDWLASE 330
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
81-166 |
9.75e-03 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270306 [Multi-domain] Cd Length: 279 Bit Score: 37.66 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709387 81 NSVEENL-KPRAAtDSLPDIVSVNASpYTATLADQGLLADIgDTQ---AWGNMLEVLQ-REWTSPGGRRYGIPSGVATTL 155
Cdd:cd13588 33 GSEDEMVaKLRSG-GGDYDVVTPSGD-ALLRLIAAGLVQPI-DTSkipNYANIDPRLRnLPWLTVDGKVYGVPYDWGANG 109
|
90
....*....|.
gi 2526709387 156 IYYNRDMFDRA 166
Cdd:cd13588 110 LAYNTKKVKTP 120
|
|
| |
