|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-348 |
5.70e-54 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 183.32 E-value: 5.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 1 MKFKTLALSCAVALGL-------GTTAANAADKEIRFDGF-PDFDSSLKVLLPDFEKET-GIKVDYLMNNHGDHHTKLTT 71
Cdd:COG1653 1 MRRLALALAAALALALaacggggSGAAAAAGKVTLTVWHTgGGEAAALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 72 NLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADKYE-ERFAPYAWAQGKgADGDMYGIPVDLGPGVMYYRTDVFE 150
Cdd:COG1653 81 ALAAGNAP-DVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDkDDFLPGALDAGT-YDGKLYGVPFNTDTLGLYYNKDLFE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 151 KAGIDVEeaiKDWDSYIAAGEKLKEQNVQlIASAADVAQAIIFTTVPEGEGL-YFDKDGNPVVTSERFVHAFEVAKEIRD 229
Cdd:COG1653 159 KAGLDPP---KTWDELLAAAKKLKAKDGV-YGFALGGKDGAAWLDLLLSAGGdLYDEDGKPAFDSPEAVEALEFLKDLVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 230 KGL--DGRILAWSNEWYEGFRNGTFATQLSGAWLLGHLNNwiaPETKGKWAVENLPDGIYGSW-----GGSFLSIPTQSD 302
Cdd:COG1653 235 DGYvpPGALGTDWDDARAAFASGKAAMMINGSWALGALKD---AAPDFDVGVAPLPGGPGGKKpasvlGGSGLAIPKGSK 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515650412 303 NPDEAWALIEYMTTDrEVQLKhFETIAAFPANITTYDDEL--FQEEME 348
Cdd:COG1653 312 NPEAAWKFLKFLTSP-EAQAK-WDALQAVLLGQKTPEEALdaAQAAAN 357
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
32-408 |
4.86e-50 |
|
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: 173.36 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 32 GFPDFDSSLKVLLPDFEKE-TGIKVDYLMNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADK 110
Cdd:cd13585 8 GQPAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAAGTAP-DVFYVDGPWVPEFASNGALLDLDDYIEKDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 111 YEERFAPYAWAQGKgADGDMYGIPVDLGPGVMYYRTDVFEKAGiDVEEAIKDWDSYIAAGEKLKEQNVQ---LIASAADV 187
Cdd:cd13585 87 LDDDFPPGLLDAGT-YDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGqygFALRGGSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 188 AQAIIFTTV-PEGEGLYFDKDGNPVVTSERFVHAFEVAKEIRDKGLDGRILAWS-NEWYEGFRNGTFATQLSGAWLLGHL 265
Cdd:cd13585 165 GQTQWYPFLwSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGgDEAVDLFASGKVAMMIDGPWALGTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 266 NNwiaPETKGKWAVENLP---DGIYGSW-GGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDE 341
Cdd:cd13585 245 KD---SKVKFKWGVAPLPagpGGKRASVlGGWGLAISKNSKHPEAAWKFIKFLTSK-ENQLKLGGAAGPAALAAAAASAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515650412 342 LFQEEMEFLggqkarLLFAEVAQNIKPVSPAQGDHVARSIILENALMEVL--DEGKDIKTALKEAERLI 408
Cdd:cd13585 321 APDAKPALA------LAAAADALAAAVPPPVPPPWPEVYPILSEALQEALlgALGKSPEEALKEAAKEI 383
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
37-404 |
3.20e-45 |
|
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: 160.56 E-value: 3.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 37 DSSLKVLLPDFEKET-GIKVDYLMNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADKYEERF 115
Cdd:cd14747 13 AELLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGP-DVVQLGNTWVAEFAAMGALEDLTPYLEDLGGDKDL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 116 APYAWAQGKGaDGDMYGIPVDLGPGVMYYRTDVFEKAGIDveEAIKDWDSYIAAGEKLKEQNVQLIASAADVAQAIIFTT 195
Cdd:cd14747 92 FPGLVDTGTV-DGKYYGVPWYADTRALFYRTDLLKKAGGD--EAPKTWDELEAAAKKIKADGPDVSGFAIPGKNDVWHNA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 196 VP----EGEGLYFDKDGNPVVTSERFVHAFEVAKEIRDKGLDGRILAW-SNEWYEGFRNGTFATQLSGAWLLGHLNNWiA 270
Cdd:cd14747 169 LPfvwgAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLEnSADVEQAFANGKVAMIISGPWEIGAIREA-G 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 271 PETKGKWAVENLPDGIYGS----WGGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQEE 346
Cdd:cd14747 248 PDLAGKWGVAPLPGGPGGGspsfAGGSNLAVFKGSKNKDLAWKFIEFLSSP-ENQAAYAKATGMLPANTSAWDDPSLAND 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515650412 347 MEFLGgqkarllFAEVAQNIKPVSPAQGDHVARSIILENALMEVLDEGKDIKTALKEA 404
Cdd:cd14747 327 PLLAV-------FAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGVGADVEDALDKA 377
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
40-405 |
6.05e-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: 152.06 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 40 LKVLLPDFEKE-TGIKVDYL-MNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADKYEE-RFA 116
Cdd:cd14748 16 LEELVDEFNKShPDIKVKAVyQGSYDDTLTKLLAALAAGTAP-DVAQVDASWVAQLADSGALEPLDDYIDKDGVDDdDFY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 117 PYAWAQGKGaDGDMYGIPVDLGPGVMYYRTDVFEKAGIDVEEAIKDWDSYIAAGEKLKEQNVQL----IASAADVAQAII 192
Cdd:cd14748 95 PAALDAGTY-DGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTgrygFALPPGDGGWTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 193 FTTVPEGEGLYFDKD-GNPVVTSERFVHAFEVAKEIRDKglDGRILAWSNEWYEG-FRNGTFATQLSGAWLLGHLNNwia 270
Cdd:cd14748 174 QALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGK--DGVSPLNDWGDAQDaFISGKVAMTINGTWSLAGIRD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 271 PETKGKWAVENLP---DGIYGSW-GGSFLSIPTQ-SDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDelfqe 345
Cdd:cd14748 249 KGAGFEYGVAPLPagkGKKGATPaGGASLVIPKGsSKKKEAAWEFIKFLTSP-ENQAKWAKATGYLPVRKSAAED----- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 346 EMEFLGGQKARLLFAEVAQNIKPVSPAQGDHVARSIILENALMEVLDEGKDIKTALKEAE 405
Cdd:cd14748 323 PEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQ 382
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
27-408 |
6.30e-41 |
|
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: 149.37 E-value: 6.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 27 EIRFDGFPDFDSS--LKVLLPDFEKETG---IKVDYLMNNHGDHHTKLTTNLATGSGAGDVIVVDVEKIGPFVGSGGLVN 101
Cdd:cd14750 1 TITFAAGSDGQEGelLKKAIAAFEKKHPdikVEIEELPASSDDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 102 LSENYGADKYEERFAPYAwaQGKGADGDMYGIPVDLGPGVMYYRTDVFEKAGidvEEAIKDWDSYIAAGEKLKEQNVQLI 181
Cdd:cd14750 81 LTEYLKEEEDDDFLPATV--EANTYDGKLYALPWFTDAGLLYYRKDLLEKYG---PEPPKTWDELLEAAKKRKAGEPGIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 182 ASAADVAQA---------IIFTTvpeGEGLYFDKDGNPVVTSERFVHAFEVAKEIRDKGL-DGRILAWS-NEWYEGFRNG 250
Cdd:cd14750 156 GYVFQGKQYeglvcnfleLLWSN---GGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGIsPKGVLTYGeEEARAAFQAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 251 TFAtqLSGAWLLG-HLNNWIAPETKGKWAVENLP--DGIYGS--WGGSFLSIPTQSDNPDEAWALIEYMTTdREVQlKHF 325
Cdd:cd14750 233 KAA--FMRNWPYAyALLQGPESAVAGKVGVAPLPagPGGGSAstLGGWNLAISANSKHKEAAWEFVKFLTS-PEVQ-KRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 326 ETIAAF-PANITTYDDELFQEEMEFLGGQKARLLFAEVaqniKPVSPAQGDhVarSIILENALMEVLDEGKDIKTALKEA 404
Cdd:cd14750 309 AINGGLpPTRRALYDDPEVLEAYPFLPALLEALENAVP----RPVTPKYPE-V--STAIQIALSAALSGQATPEEALKQA 381
|
....
gi 515650412 405 ERLI 408
Cdd:cd14750 382 QEKL 385
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-409 |
6.54e-41 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 149.71 E-value: 6.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 1 MKFKT---LALSCAVALGL----------GTTAANAADKEIRFDGFPDFDSSLKVLLPDFEKETGIKVDYLMNNHGDHHT 67
Cdd:COG2182 1 MKRRLlaaLALALALALALaacgsgssssGSSSAAGAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 68 KLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSEnygADKYEERFAPYAWAQGKgADGDMYGIPVDLGPGVMYYRTD 147
Cdd:COG2182 81 KLTTAAPAGKGP-DVFVGAHDWLGELAEAGLLAPLDD---DLADKDDFLPAALDAVT-YDGKLYGVPYAVETLALYYNKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 148 VFEkagidvEEAIKDWDSYIAAGEKLKEQNVQLIAsaADVAQAiiFTTVP--EGEGLY-FDKDGN----PVVTSERFVHA 220
Cdd:COG2182 156 LVK------AEPPKTWDELIAAAKKLTAAGKYGLA--YDAGDA--YYFYPflAAFGGYlFGKDGDdpkdVGLNSPGAVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 221 FEVAKEIRDKGLDGRILAWSNEWyEGFRNGTFATQLSGAWLLGHlnnwIAPETKGKWAVENLPDGIYGSW-----GGSFL 295
Cdd:COG2182 226 LEYLKDLIKDGVLPADADYDAAD-ALFAEGKAAMIINGPWAAAD----LKKALGIDYGVAPLPTLAGGKPakpfvGVKGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 296 SIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQEEmEFLGGqkarllFAEVAQN--IKPVSPAQ 373
Cdd:COG2182 301 GVSAYSKNKEAAQEFAEYLTSP-EAQKALFEATGRIPANKAAAEDAEVKAD-PLIAA------FAEQAEYavPMPNIPEM 372
|
410 420 430
....*....|....*....|....*....|....*.
gi 515650412 374 GDhVarSIILENALMEVLDEGKDIKTALKEAERLIK 409
Cdd:COG2182 373 GA-V--WTPLGTALQAIASGKADPAEALDAAQKQIE 405
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-345 |
1.15e-32 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 124.44 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 46 DFEKETGIKVDYLMNNHGDHHTKLTTNLATGSGAG-DVIVVDVEKIGPFVGSGGLVNLSENYGADKYEERFAPYawaqgk 124
Cdd:pfam13416 5 AFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDlDVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 125 GADGDMYGIPVDLG-PGVMYYRTDVFEKAGIDVeeaiKDWDSYIAAGEKLKeQNVQLIASAADVAQAIifttvPEGEGLY 203
Cdd:pfam13416 79 GYDGKLYGVPYAAStPTVLYYNKDLLKKAGEDP----KTWDELLAAAAKLK-GKTGLTDPATGWLLWA-----LLADGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 204 FDKDGNPVVTSERfvhAFEVAKEIRDkglDGRILAWSNEWYEGFRNGTFATQLSGAWLLGHlnnwiAPETKGKWAVENLP 283
Cdd:pfam13416 149 LTDDGKGVEALDE---ALAYLKKLKD---NGKVYNTGADAVQLFANGEVAMTVNGTWAAAA-----AKKAGKKLGAVVPK 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515650412 284 DGIYgsWGGSFLSIPTQSDNPDE-AWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQE 345
Cdd:pfam13416 218 DGSF--LGGKGLVVPAGAKDPRLaALDFIKFLTSP-ENQAALAEDTGYIPANKSAALSDEVKA 277
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
37-317 |
2.39e-26 |
|
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: 107.50 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 37 DSSLKVLLPDFEKE-TGIKVDYLMNNHGDHHTKLTTNLATGSGAGDVIVVDVEKIGPFVGSGGLVNLSenygadkyeerf 115
Cdd:pfam01547 7 AAALQALVKEFEKEhPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLD------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 116 aPYAWAQGKGADGDMYGIPVDLGPGVMYYRTDVFEKAGIDVeeaIKDWDSYIAAGEKLKEQN---VQLIASAADVAQAII 192
Cdd:pfam01547 75 -DYVANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP---PKTWDELLEAAKKLKEKGkspGGAGGGDASGTLGYF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 193 FTTVPEGEGLYFDKDGNPVVTSERFVHAFEVAKEIRDKGLDGRILAW-------SNEWYEGFRNGTFATQLSGAWLLGHL 265
Cdd:pfam01547 151 TLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNpgvagadGREALALFEQGKAAMGIVGPWAALAA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 266 NNW--------IAPETKGKWAVENLPDGIYGSWGGSFLSIPTQSDNPDEAWALIEYMTTD 317
Cdd:pfam01547 231 NKVklkvafaaPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
46-409 |
1.24e-25 |
|
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: 107.08 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 46 DFEKET-GIKVDYLMNNHGDHHTKLTTNLATGSGaGDVI-VVDVEKIGPFVGSGGLVNLSENYGADKYEERFAPYAWAQG 123
Cdd:cd14749 23 DFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEG-PDVFnLWPGGWLAEFVKAGLLLPLTDYLDPNGVDKRFLPGLADAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 124 KGaDGDMYGIPVDLGPGVMYYRTDVFEKAGIDveEAIKDWDSYIAAGEKLKEQNVQLIASA----ADVAQAIIFTTVP-E 198
Cdd:cd14749 102 TF-NGKVYGIPFAARALALFYNKDLFEEAGGV--KPPKTWDELIEAAKKDKFKAKGQTGFGlllgAQGGHWYFQYLVRqA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 199 GEGLYFDKDGNPV-VTSERFVHAFEVAKEIRDKGLDGRilAWSNEWYEG----FRNGTFATQLSGAWLLGHLNNwiaPET 273
Cdd:cd14749 179 GGGPLSDDGSGKAtFNDPAFVQALQKLQDLVKAGAFQE--GFEGIDYDDagqaFAQGKAAMNIGGSWDLGAIKA---GEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 274 KGKWAVENLP----DGIYGSWGGSF--LSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPA---NITTYDDELFQ 344
Cdd:cd14749 254 GGKIGVFPFPtvgkGAQTSTIGGSDwaIAISANGKKKEAAVKFLKYLTSP-EVMKQYLEDVGLLPAkevVAKDEDPDPVA 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515650412 345 EEMEFLGG--QKARLLFAEvaqnikPVSPAQGDHVArsiileNALMEVLDEGKDIKTALKEAERLIK 409
Cdd:cd14749 333 ILGPFADVlnAAGSTPFLD------EYWPAAAQVHK------DAVQKLLTGKIDPEQVVKQAQSAAA 387
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
41-409 |
2.20e-25 |
|
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: 106.31 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 41 KVLLPDFEKET-GIKVDYLMNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADKYEERFA-PY 118
Cdd:cd14751 17 EKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAP-DVMRADIAWVPEFAKLGYLQPLDGTPAFDDIVDYLPgPM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 119 AWAQgkgADGDMYGIPVDLGPGVMYYRTDVFEKAGIDVEeaiKDWDSYIAAGEKLKE-QNVQLIASAADVAQAIIFTTVP 197
Cdd:cd14751 96 ETNR---YNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP---KTMDELVAAAKAIKKkKGRYGLYISGDGPYWLLPFLWS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 198 EGEGLYFDKDGNPVVTSERFVHAFEVAKEIRDKGLdgrILAWSNEWY----EGFRNGTFATQLSGAWLLGHLNNWIAPET 273
Cdd:cd14751 170 FGGDLTDEKKATGYLNSPESVRALETIVDLYDEGA---ITPCASGGYpnmqDGFKSGRYAMIVNGPWAYADILGGKEFKD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 274 KGKWAVENLPDGIYGS---WGGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQEEMEFL 350
Cdd:cd14751 247 PDNLGIAPVPAGPGGSgspVGGEDLVIFKGSKNKDAAWKFVKFMSSA-EAQALTAAKLGLLPTRTSAYESPEVANNPMVA 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 515650412 351 GGQKArllfAEVAQNiKPVSPAQGdhvARSIILENALMEVLDEGKDIKTALKEAERLIK 409
Cdd:cd14751 326 AFKPA----LETAVP-RPPIPEWG---ELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
47-408 |
3.34e-19 |
|
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: 88.51 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 47 FEKETGIKVDYLMNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSeNYGADKYEerFAPYAWAQGKgA 126
Cdd:cd13586 22 FEKKYGIKVEVVYVDSGDTREKFITAGPAGKGP-DVFFGPHDWLGELAAAGLLAPIP-EYLAVKIK--NLPVALAAVT-Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 127 DGDMYGIPVDLGPGVMYYRTDvfekagiDVEEAIKDWDSYIAAGEKLKEQNVQLIASAADVAQAIIFTTVPEGEGLY-FD 205
Cdd:cd13586 97 NGKLYGVPVSVETIALFYNKD-------LVPEPPKTWEELIALAKKFNDKAGGKYGFAYDQTNPYFSYPFLAAFGGYvFG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 206 KDGNPV----VTSERFVHAFEVAKEIRDKGldgRILAWSNEwYEG----FRNGTFATQLSGAWLLGHLNnwiapETKGKW 277
Cdd:cd13586 170 ENGGDPtdigLNNEGAVKGLKFIKDLKKKY---KVLPPDLD-YDIadalFKEGKAAMIINGPWDLADYK-----DAGINF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 278 AVENLPDGIYGSWGGSFL-----SIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQEEmEFLGG 352
Cdd:cd13586 241 GVAPLPTLPGGKQAAPFVgvqgaFVSAYSKNKEAAVEFAEYLTSD-EAQLLLFEKTGRIPALKDALNDAAVKND-PLVKA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515650412 353 qkarllFAEVAQ------NIKPVSPAQGDhvarsiiLENALMEVLDEGKDIKTALKEAERLI 408
Cdd:cd13586 319 ------FAEQAQygvpmpNIPEMAAVWDA-------MGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
40-408 |
6.00e-18 |
|
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: 84.77 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 40 LKVLLPDFEKET-GIKVDyLMNNHGDHHTKLTTNLATGSGAGDVIVVDVEKIGPFVGSGGLVNLSENYGADKYEERFAPY 118
Cdd:cd13522 16 VNELIAKFEKAYpGITVE-VTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSKSGKYAPNTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 119 AWAQgkgaDGDMYGIPVDLGPGVMYYRTDVFEKagidveEAIKDWDSYIAAGEKLKEQNVqlIASAADVAQAIIFTTVPE 198
Cdd:cd13522 95 AMKL----NGKLYGVPVSVGAHLMYYNKKLVPK------NPPKTWQELIALAQGLKAKNV--WGLVYNQNEPYFFAAWIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 199 GEGLYFDKDGN----PVVTSERFVHAFEVAKEIRDKgldGRILAwSNEWYEG----FRNGTFATQLSGAWLLGHLNNwia 270
Cdd:cd13522 163 GFGGQVFKANNgknnPTLDTPGAVEALQFLVDLKSK---YKIMP-PETDYSIadalFKAGKAAMIINGPWDLGDYRQ--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 271 pETKGKWAVENLPDGIYGSW-----GGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQE 345
Cdd:cd13522 236 -ALKINLGVAPLPTFSGTKHaapfvGGKGFGINKESQNKAAAVEFVKYLTSY-QAQLVLFDDAGDIPANLQAYESPAVQN 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515650412 346 EMeflgGQKARLLFAEVAQnIKPVSPAQGdhvARSIILENALMEVLDEGKDIKTALKEAERLI 408
Cdd:cd13522 314 KP----AQKASAEQAAYGV-PMPNIPEMR---AVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
2-347 |
1.36e-13 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 71.48 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 2 KFKTLALSCAVALGLGTTAANAADKEIRFDGFPDFDSslKVLLPDFEKETGIKVDY-LMNNHGDHHTKLttnLATGSGAg 80
Cdd:COG0687 5 SLLGLAAAALAAALAGGAPAAAAEGTLNVYNWGGYID--PDVLEPFEKETGIKVVYdTYDSNEEMLAKL---RAGGSGY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 81 DVIVVDVEKIGPFVGSGGLVNLseNYGADKYEERFAPyAWAQGKGADGDMYGIPVDLGPGVMYYRTDVfekagidVEEAI 160
Cdd:COG0687 79 DVVVPSDYFVARLIKAGLLQPL--DKSKLPNLANLDP-RFKDPPFDPGNVYGVPYTWGTTGIAYNTDK-------VKEPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 161 KDWDSYIAagEKLKEQnVQLIASAADVAQAI-------IFTTVPEGeglyFDKdgnpvvtserfvhAFEVAKEIRDkgld 233
Cdd:COG0687 149 TSWADLWD--PEYKGK-VALLDDPREVLGAAllylgydPNSTDPAD----LDA-------------AFELLIELKP---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 234 gRILAWSN---EWYEGFRNGTFATQL--SGAWLLGHLNN----WIAPEtkgkwavenlpDGIYGsWGGSFlSIPTQSDNP 304
Cdd:COG0687 205 -NVRAFWSdgaEYIQLLASGEVDLAVgwSGDALALRAEGppiaYVIPK-----------EGALL-WFDNM-AIPKGAPNP 270
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 515650412 305 DEAWALIEYMtTDREVQLKHFETIAAFPANITTydDELFQEEM 347
Cdd:COG0687 271 DLAYAFINFM-LSPEVAAALAEYVGYAPPNKAA--RELLPPEL 310
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
46-409 |
2.33e-10 |
|
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: 61.73 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 46 DFEKETGIKVDYLMNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENYGADKyeeRFAPYAwAQGKG 125
Cdd:cd13658 21 QYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGP-DVMVAPHDRIGSAVLQGLLSPIKLSKDKKK---GFTDQA-LKALT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 126 ADGDMYGIPVDLGPGVMYYRTDVFEKAgidvEEAIKDWDSYIAAGEKLKEQNVQLIASAADvaqaiIFTTVP--EGEGLY 203
Cdd:cd13658 96 YDGKLYGLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQYGFLADATN-----FYYSYGllAGNGGY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 204 -FDKDGNPV------VTSERFVHAFEVAKEIRDKGLdgrilawsneWYEG---------FRNGTFATQLSGAWLL----- 262
Cdd:cd13658 167 iFKKNGSDLdindigLNSPGAVKAVKFLKKWYTEGY----------LPKGmtgdviqglFKEGKAAAVIDGPWAIqeyqe 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 263 GHLNNWIAPetkgkwaVENLPDGIYGS--WGGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDD 340
Cdd:cd13658 237 AGVNYGVAP-------LPTLPNGKPMApfLGVKGWYLSAYSKHKEWAQKFMEFLTSK-ENLKKRYDETNEIPPRKDVRSD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515650412 341 ELFQEE--MEFLGGQKARllfAEVAQNIKPVS----PAqgdhvarsiilENALMEVLDEGKDIKTALKEAERLIK 409
Cdd:cd13658 309 PEIKNNplTSAFAKQASR---AVPMPNIPEMGavwePA-----------NNALFFILSGKKTPKQALNDAVNDIK 369
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
37-408 |
4.43e-10 |
|
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: 60.85 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 37 DSSLKVLLPDFEKETGI---KVDYlmNNHGDHHTKLTTNLATGSGAgDVIVVDVEKIGPFVGSGGLVNLSeNYGADKYEE 113
Cdd:cd13657 13 EDALQQIIDEFEAKYPVpnvKVPF--EKKPDLQNKLLTAIPAGEGP-DLFIWAHDWIGQFAEAGLLVPIS-DYLSEDDFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 114 RFAPYAwAQGKGADGDMYGIPVDLGPGVMYYRTDVfekagidVEEAIKDWDSYIAAGEKLKEQNVQLIASAADVAQAIIF 193
Cdd:cd13657 89 NYLPTA-VEAVTYKGKVYGLPEAYETVALIYNKAL-------VDQPPETTDELLAIMKDHTDPAAGSYGLAYQVSDAYFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 194 TTVPEGEG-LYFDKDG-NPVVTSERFVHAFEVAKEIRDKGLDgrilawSNEWYEG----FRNGTFATQLSGAWLLGHLNN 267
Cdd:cd13657 161 SAWIFGFGgYYFDDETdKPGLDTPETIKGIQFLKDFSWPYMP------SDPSYNTqtslFNEGKAAMIINGPWFIGGIKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 268 WIApetkgKWAVENLPDGI-------YGSWGGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDD 340
Cdd:cd13657 235 AGI-----DLGVAPLPTVDgtnpprpYSGVEGIYVTKYAERKNKEAALDFAKFFTTA-EASKILADENGYVPAATNAYDD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 341 ELFQEEMEFLGgqkarllFAEVAQNIK--PVSPaQGDHVARSIilENALMEVLDEGKDIKTALKEAERLI 408
Cdd:cd13657 309 AEVAADPVIAA-------FKAQAEHGVpmPNSP-EMASVWGPV--TLALAAVYQGGQDPQEALAAAQQEI 368
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
48-394 |
7.54e-10 |
|
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: 60.42 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 48 EKETGIKVDYLMNNHGDHHTKLTTNLATGSgAGDVIVVDVEKIG-PFVGSGGLVNLSENYgaDKYEERFAPYAWAQGKGA 126
Cdd:cd13580 29 EEKTNIDVKVKWVPDSSYDEKLNLALASGD-LPDIVVVNDPQLSiTLVKQGALWDLTDYL--DKYYPNLKKIIEQEGWDS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 127 ---DGDMYGIPV---DLGPGVMYYRTDVFEKAGIdveEAIKDWDSYIAAGEKLKEQNVQL--------IASAADVAQAII 192
Cdd:cd13580 106 asvDGKIYGIPRkrpLIGRNGLWIRKDWLDKLGL---EVPKTLDELYEVAKAFTEKDPDGngkkdtygLTDTKDLIGSGF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 193 FTTVP----EGEGLYFDKDGN--PVVTSERFVHAFEVAKEIRDKGL------------------DGRILAWSNEWYEGFR 248
Cdd:cd13580 183 TGLFGafgaPPNNWWKDEDGKlvPGSIQPEMKEALKFLKKLYKEGLidpefavndgtkanekfiSGKAGIFVGNWWDPAW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 249 N-GTFATQLSGAwllghlnNWIA-PETKGkwavenlPDGIYGSWGGS----FLSIPTQSDNPDEAWALIEYMtTDREVQL 322
Cdd:cd13580 263 PqASLKKNDPDA-------EWVAvPIPSG-------PDGKYGVWAESgvngFFVIPKKSKKPEAILKLLDFL-SDPEVQK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 323 --------KHFETIAAFPANITTYDD-ELFQEEMEFLGGQKArLLFAEVAQNIKPVSpaQGDHVARSIILENALMEVLDE 393
Cdd:cd13580 328 lldygiegVHYTVKDGGPVNIIPPDKqEVGDATLDYFQGSLA-LEKYKLTNNGERKS--DAKKEALDERVVNANDEENEN 404
|
.
gi 515650412 394 G 394
Cdd:cd13580 405 I 405
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
47-175 |
1.18e-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: 50.43 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 47 FEKETGIKVDYLMNNHGDHHTKLTTNLATGSgAGDVI-VVDVEKIGPFVGSGGLVNLSE------NYgADKYEERFAPYA 119
Cdd:cd13583 26 IEEKTNVKFKRTPIPSSDYETKRSLLIASGD-APDIIpVLYPGEENEFVASGALLPISDyldympNY-KKYVEKWGLGKE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 120 WAQGKGADGDMYGIPV-DLGPGVMY---YRTDVFEKAGIDVEEAikdWDSYIAAGEKLKE 175
Cdd:cd13583 104 LATGRQSDGKYYSLPGlHEDPGVQYsflYRKDIFEKAGIKIPTT---WDEFYAALKKLKE 160
|
|
| PBP2_AlgQ_like_3 |
cd13582 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
47-321 |
1.01e-05 |
|
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: 270300 [Multi-domain] Cd Length: 504 Bit Score: 47.70 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 47 FEKETG--IKVDYLMnnhGDHHTKLTTNLATGSgAGDVIVVDVEkIGPFVGSGGLV-----------NLSENYGaDKYEE 113
Cdd:cd13582 26 ITELTGvtLEIEYLV---GGEKQKIGLMIASGD-LPDLIYAKGD-TDKLIEAGALVplddliekygpNIKKWYG-DYLLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 114 RFAPyawaqgkgADGDMYGIP-------VDLGPGVMYYRTDVFEKAGIDVeeaIKDWDSYIAAGEKLKEQNVQL-----I 181
Cdd:cd13582 100 KLRS--------EDGHIYYLPnyrvedaPWYPNGGFWLQHDVLKELGYPK---IKTLDDYENLIKDYKKKYPTIngqptI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 182 ASAADVAQAIIFTTVPEGEGLYFDKDGNPVV----TSERFVH-AFEVAKE-------IRDKGL----------------- 232
Cdd:cd13582 169 GFTALTDDWRFLISVTNPAFLAGYPNDGEVYvdpkTLKAKFHyTRPYYKEyykwlneLWNEGLldkesftqkydqylaki 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 233 -DGRILA-WSNEWYEGFRNGTFATQLSGAWLLGhlnnwIAPETKGKwAVENLPDGIYGSWGGSFLSIPTQSDNPDEAWAL 310
Cdd:cd13582 249 aSGRVLGfYDAGWDIGNAITALKAKGKDERLYA-----YYPVAVGV-DDKDYNYGDPGYLGGDGIAITKSCKDPERAFKF 322
|
330
....*....|.
gi 515650412 311 IEYMTTDrEVQ 321
Cdd:cd13582 323 LDWLASE-EAQ 332
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
43-334 |
1.12e-05 |
|
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: 46.84 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 43 LLPDFEKETGIKVDYlmnnhgdhhTKLTTN------LATGSGAG-DVIVVDVEKIGPFVGSGGLVNLSENY--GADKYEE 113
Cdd:cd13590 15 VLKAFEKETGVKVNY---------DTYDSNeemlakLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlpNLKNLDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 114 RFAPYAWaqgkgADGDMYGIPVDLGPGVMYYRTDVfekagidVEEAIKDWDSYIAAgEKLKeQNVQLIASAADVAQAI-- 191
Cdd:cd13590 86 QFLNPPY-----DPGNRYSVPYQWGTTGIAYNKDK-------VKEPPTSWDLDLWD-PALK-GRIAMLDDAREVLGAAll 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 192 -----IFTTVPEgeglYFDKdgnpvvtserfvhAFEVAKEIRdkgldGRILAW-SNEWYEGFRNGTFATQL--SGAWLLG 263
Cdd:cd13590 152 algysPNTTDPA----ELAA-------------AAELLIKQK-----PNVRAFdSDSYVQDLASGEIWLAQawSGDALQA 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515650412 264 HLNN----WIAPETKGKWAVENlpdgiygswggsfLSIPTQSDNPDEAWALIEYMtTDREVQLKHFETIAAFPAN 334
Cdd:cd13590 210 NRENpnlkFVIPKEGGLLWVDN-------------MAIPKGAPNPELAHAFINFL-LDPEVAAKNAEYIGYATPN 270
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-181 |
1.12e-04 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 44.23 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 1 MKFKTLALSCAVALGLgTTAANAADKE----IRFDGfpdfDSSLKVLL---PDFEKETGIKVdyLMNNHGDHHTKLTTNL 73
Cdd:PRK09474 5 KGLRTLALSALATLMF-SASALAKIEEgklvIWING----DKGYNGLAevgKKFEKDTGIKV--TVEHPDKLEEKFPQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 74 ATGSGAgDVIVVDVEKIGPFVGSGGLVNLSENygaDKYEERFAPYAWaQGKGADGDMYGIPVDLGPGVMYYRTDVfekag 153
Cdd:PRK09474 78 ATGDGP-DIIFWAHDRFGGYAQSGLLAEVTPS---KAFKDKLVPFTW-DAVRYNGKLIGYPIAVEALSLIYNKDL----- 147
|
170 180
....*....|....*....|....*...
gi 515650412 154 idVEEAIKDWDSYIAAGEKLKEQNVQLI 181
Cdd:PRK09474 148 --VPTPPKTWEEIPALDKELKAKGKSAI 173
|
|
| TupB |
COG2998 |
ABC-type tungstate transport system, permease component TupA [Inorganic ion transport and ... |
1-85 |
1.07e-03 |
|
ABC-type tungstate transport system, permease component TupA [Inorganic ion transport and metabolism];
Pssm-ID: 442236 Cd Length: 272 Bit Score: 40.54 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 1 MKFKTLALSCAVALGLGTT-AANAADKEIR------FDgfpdfDSSL-KVLLPDFEKETGIKVDYlmnnhgdhhtklttn 72
Cdd:COG2998 1 MKRRLLLLLLLLLLALALAgAAAAAAESLRlatttsTE-----DSGLlDYLLPAFEKKTGIEVKV--------------- 60
|
90 100
....*....|....*....|
gi 515650412 73 LATGSGA-------GDVIVV 85
Cdd:COG2998 61 VAVGTGQalelgrrGDADVL 80
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
2-103 |
1.69e-03 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 40.44 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 2 KFKTLALSCAVALGLGTTAANAADKEIRF---DGFPDFdssLKVLLPDFEKETGIKVDYLMNNHGDHHTKLttNLATGSG 78
Cdd:PRK15046 11 AAMKLAAAAAAAAFGGGAAPAWAADAVTVysaDGLEDW---YQDVFPAFTKATGIKVNYVEAGSGEVVNRA--AKEKSNP 85
|
90 100
....*....|....*....|....*....
gi 515650412 79 AGDVIVVdvekIGPFV----GSGGLVNLS 103
Cdd:PRK15046 86 QADVLVT----LPPFIqqaaAEGLLQPYS 110
|
|
| PBP2_polyamine_2 |
cd13587 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
43-338 |
1.78e-03 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type 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: 270305 [Multi-domain] Cd Length: 292 Bit Score: 40.11 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 43 LLPDFEKETGIKVDY-LMNNHGDHHTKLTtnlATGSGAGDVIVVDVEKIGPFVGSGGLVNLSE-NYGADKYeerfaPYAW 120
Cdd:cd13587 15 LLEKFENETGIKVQVtTSNNNEEMISKLR---ATGGGGFDLAQPSQRIAPNYEEFGLYQPIDEsKIKVAQF-----PPSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 121 AQGKGA----DGDMYGIPVDLGPGVMYYRTDVFEKAgidveeaikdwdSYIAAGEKLKEQNvqliASAADVAQAIIFTTV 196
Cdd:cd13587 87 LESTKLgttiNGKRYAVPFDWGTEGLTVNSTKAPDV------------SGFSYGDLWAPEY----AGKVAYRLKSPLTGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 197 pegeGLYFDKDGNpvvtsERFVHAFEVAKEIRDKGLDGRILAW--------------SNEWYEGFR-NGTFATQL--SGA 259
Cdd:cd13587 151 ----GLYADATGE-----DPFNRYLDYKDEAKYQKILDQVLQFlierkanvkaywnnADEALAAFRsGGCVIGQTwdSTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 260 WLLGHLN---NWIAPETkgkwavenlpdGIYGsWGGSFlSIPTQSDNPDEAWALIEYMTTDRevqlkhfetIAAFPANIT 336
Cdd:cd13587 222 LKLNRENppiDYGAPKE-----------GALG-WIDTF-AIPAKAENVDQAYAFINFMLRPE---------IAAMFTNAT 279
|
..
gi 515650412 337 TY 338
Cdd:cd13587 280 GY 281
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
41-153 |
1.98e-03 |
|
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: 39.90 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 41 KVLLPDFEKETGIKVDYLMNNHGDHHTKLTTNlatgSGAGDVIVVDVEkiGPFVGSGGLVNLSENYGADKYEERFAPYAW 120
Cdd:cd13589 17 KAVIEPFEKETGIKVVYDTGTSADRLAKLQAQ----AGNPQWDVVDLD--DGDAARAIAEGLLEPLDYSKIPNAAKDKAP 90
|
90 100 110
....*....|....*....|....*....|...
gi 515650412 121 AqgkgADGDMYGIPVDLGPGVMYYRTDVFEKAG 153
Cdd:cd13589 91 A----ALKTGYGVGYTLYSTGIAYNTDKFKEPP 119
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
43-367 |
3.86e-03 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 38.76 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 43 LLPDFEKETGIKVDYLMNNHGDHHTKLTTNlaTGSGAGDVIVVdvekigpfVGSGGLVNLsenygadKYEERFAPYAWAQ 122
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLARLKAE--GGNPPADVVWS--------GDADALEQL-------ANEGLLQPYKSPE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 123 GKG-----ADGDMYGIPVDLGPGVMYYRTDVFEKagidvEEAIKDWDSYiaAGEKLKEQnvqlIA----SAADVAQAIIF 193
Cdd:COG1840 64 LDAipaefRDPDGYWFGFSVRARVIVYNTDLLKE-----LGVPKSWEDL--LDPEYKGK----IAmadpSSSGTGYLLVA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 194 T-TVPEGEGLYFD-----KDGNPVVTSerfvHAFEVAKEIrdkgLDGRI-LAWSNEWYegfrngTFATQLSGAWLlghln 266
Cdd:COG1840 133 AlLQAFGEEKGWEwlkglAANGARVTG----SSSAVAKAV----ASGEVaIGIVNSYY------ALRAKAKGAPV----- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515650412 267 NWIAPEtkgkwavenlpDGIYgsWGGSFLSIPTQSDNPDEAWALIEYMTTDrEVQLKHFETIAAFPANITTYDDELFQEe 346
Cdd:COG1840 194 EVVFPE-----------DGTL--VNPSGAAILKGAPNPEAAKLFIDFLLSD-EGQELLAEEGYEYPVRPDVEPPEGLPP- 258
|
330 340
....*....|....*....|.
gi 515650412 347 mefLGGQKARLLFAEVAQNIK 367
Cdd:COG1840 259 ---LGELKLIDDDDKAAENRE 276
|
|
| DctP |
COG1638 |
TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and ... |
1-57 |
4.25e-03 |
|
TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441245 [Multi-domain] Cd Length: 329 Bit Score: 39.05 E-value: 4.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515650412 1 MKFKTLALSCAVALGLGTTAANAADKEIRF-DGFPDfDSSLKVLLPDF----EKETG--IKVDY 57
Cdd:COG1638 1 MKRKLLAAALAAALALAAAAAAAAAVTLKLaHVLPP-GHPWGKAAEKFaeevEERTGgrIKVEV 63
|
|
| |
