|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
3-437 |
2.54e-52 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 179.47 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 3 MKKFAsLAMLGASVLGLAACGGKSqkeaSESKSDAAKTEITWWAFpvftqekaEDGVGTYEKKLIAAFEKANPEIKVKLE 82
Cdd:COG1653 1 MRRLA-LALAAALALALAACGGGG----SGAAAAAGKVTLTVWHT--------GGGEAAALEALIKEFEAEHPGIKVEVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 83 TIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDLFTKE-FTKDVNNDKLIQASKAGDTAYMYPISSAP 161
Cdd:COG1653 68 SVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgLDKDDFLPGALDAGTYDGKLYGVPFNTDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 162 FYMALNKKMLKDAGvldlVKEGWTTDDFEKVLKALKDKGYNPGSFFANGQGgdqgprAFFANLYSSHITD--DKVTKYTT 239
Cdd:COG1653 148 LGLYYNKDLFEKAG----LDPPKTWDELLAAAKKLKAKDGVYGFALGGKDG------AAWLDLLLSAGGDlyDEDGKPAF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 240 DDANSIKAMTKISNWIKDGLMMNGS-QYDGSADIQNFANGQTSFTILWAPAQPGIQAkllEASKVDYLEIPFPSDDGKPE 318
Cdd:COG1653 218 DSPEAVEALEFLKDLVKDGYVPPGAlGTDWDDARAAFASGKAAMMINGSWALGALKD---AAPDFDVGVAPLPGGPGGKK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 319 LEYLVNGFAVFNNKDEQKVAASKTFIQFIADDKEWgpknvvrtgafpvrtsygdlykdkrmekiaewtkfyspyyntidg 398
Cdd:COG1653 295 PASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQ--------------------------------------------- 329
|
410 420 430
....*....|....*....|....*....|....*....
gi 1611951076 399 faemrtLWFPMVQAISNGDEKPEDALKAFTEKANKTIKK 437
Cdd:COG1653 330 ------AKWDALQAVLLGQKTPEEALDAAQAAANAALAR 362
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
41-431 |
1.11e-46 |
|
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: 165.27 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 41 EITWWAFPVFTQEKAEdgvgtyeKKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNG 120
Cdd:cd13585 1 TLTFWDWGQPAETAAL-------KKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 121 KLADLNDLFTKEFTKDVNNDKLIQASKAGDTAYMYPISSAPFYMALNKKMLKDAGvlDLVKEGWTTDDFEKVLKALKDKG 200
Cdd:cd13585 74 ALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG--PGPKPPWTWDELLEAAKKLTDKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 201 YNPGSFFANGQGGDQGPRAFFANLYSSHITDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDGSADIQNFANGQT 280
Cdd:cd13585 152 GGQYGFALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 281 SFTILWAPAQPGIQAKLLEAsKVDYleIPFPSDDGKPELEYL-VNGFAVFnnKDEQKVAASKTFIQFIADD---KEWGPK 356
Cdd:cd13585 232 AMMIDGPWALGTLKDSKVKF-KWGV--APLPAGPGGKRASVLgGWGLAIS--KNSKHPEAAWKFIKFLTSKenqLKLGGA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1611951076 357 NVVRTGAFPVRTSYGDLYKDKRMEKIAEWTKFYSPYYNTIDGFAEMRTLWFPMVQAISNGDEK--PEDALKAFTEKA 431
Cdd:cd13585 307 AGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGksPEEALKEAAKEI 383
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-437 |
5.99e-45 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 161.27 E-value: 5.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 1 MNMKKFASLAMLGASVLGLAACGGKSQKEASESKSDAAKTeITWWAfpvfTQEKAEdgvgtYEKKLIAAFEKAnPEIKVK 80
Cdd:COG2182 1 MKRRLLAALALALALALALAACGSGSSSSGSSSAAGAGGT-LTVWV----DDDEAE-----ALEEAAAAFEEE-PGIKVK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 81 LETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDLFTKeftKDVNNDKLIQASKAGDTAYMYPISS- 159
Cdd:COG2182 70 VVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLAD---KDDFLPAALDAVTYDGKLYGVPYAVe 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 160 --APFYmalNKKMLKDagvlDLVKegwTTDDFEKVLKALKDKG-----YNPGSF-----FANGQGGDqgpraFFANlyss 227
Cdd:COG2182 147 tlALYY---NKDLVKA----EPPK---TWDELIAAAKKLTAAGkyglaYDAGDAyyfypFLAAFGGY-----LFGK---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 228 hiTDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDGSadIQNFANGQTSFTILWapaqPGIQAKLLEASKVDYLE 307
Cdd:COG2182 208 --DGDDPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAA--DALFAEGKAAMIING----PWAAADLKKALGIDYGV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 308 IPFPS-DDGKPELEYL-VNGFAVfNNKDEQKVAASKtFIQFIAddkewGPKNVVR----TGAFPVRTSYGD---LYKDKR 378
Cdd:COG2182 280 APLPTlAGGKPAKPFVgVKGFGV-SAYSKNKEAAQE-FAEYLT-----SPEAQKAlfeaTGRIPANKAAAEdaeVKADPL 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1611951076 379 MEKIAEWTKFYSPYYNTidgfAEMRTLWFPM---VQAISNGDEKPEDALKAFTEKANKTIKK 437
Cdd:COG2182 353 IAAFAEQAEYAVPMPNI----PEMGAVWTPLgtaLQAIASGKADPAEALDAAQKQIEAAIAQ 410
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
41-431 |
6.21e-36 |
|
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: 136.27 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 41 EITWWAFpvftqekAEDGVGTYEKKLIAAFEKANPEIKVKLETI-DFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKN 119
Cdd:cd14748 1 EITFWHG-------MSGPDGKALEELVDEFNKSHPDIKVKAVYQgSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 120 GKLADLNDLFTKEFTKDVN-NDKLIQASKAGDTAYMYPISSAPFYMALNKKMLKDAGvLDLVKEGWTTDDFEKVLKALKD 198
Cdd:cd14748 74 GALEPLDDYIDKDGVDDDDfYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAG-LDPEKPPKTWDELEEAAKKLKD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 199 KGYNPGSF-FANGQGGDQGPRAFFANLYSSHITDDKVTKYTTDDANSIKAMTKISNWI-KDGLMMNGSQYDGSadiQNFA 276
Cdd:cd14748 153 KGGKTGRYgFALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVgKDGVSPLNDWGDAQ---DAFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 277 NGQTSFTILWAPAQPGIQAKlleASKVDYLEIPFPSDDGKPELEYLV-NGFAVFNNKDEQKvAASKTFIQFIAdDKEWGP 355
Cdd:cd14748 230 SGKVAMTINGTWSLAGIRDK---GAGFEYGVAPLPAGKGKKGATPAGgASLVIPKGSSKKK-EAAWEFIKFLT-SPENQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 356 KNVVRTGAFPVRTS-----YGDLYKDKRMEKIAEWTKFYSPYYNTIDGFAEMRTLWFPMVQAISNGDEKPEDALKAFTEK 430
Cdd:cd14748 305 KWAKATGYLPVRKSaaedpEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
|
.
gi 1611951076 431 A 431
Cdd:cd14748 385 I 385
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
41-433 |
1.21e-29 |
|
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: 119.02 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 41 EITWWAFPVFTQEKAedgvgtYEKKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQ-YGKN 119
Cdd:cd14749 1 TITYWQYFTGDTKKK------YMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAeFVKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 120 GKLADLNDLFTKEFTKDVNNDKLIQASKAGDTAYMYPISSAPFYMALNKKMLKDAGVLDLVKegwTTDDFEKVLKALKDK 199
Cdd:cd14749 75 GLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPK---TWDELIEAAKKDKFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 200 GYNPGSFfaNGQGGDQGPRAFFANLYSSH----ITDDKVTKYTTDDANSIKAMTKISNWIKDGLM-MNGSQYDGSADIQN 274
Cdd:cd14749 152 AKGQTGF--GLLLGAQGGHWYFQYLVRQAgggpLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFqEGFEGIDYDDAGQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 275 FANGQTSFTI--LWA-----PAQPGIqaklleasKVDYLEIPFPSDDGKPELEYlVNGFAVFNNKDEQKVAASKTFIQFI 347
Cdd:cd14749 230 FAQGKAAMNIggSWDlgaikAGEPGG--------KIGVFPFPTVGKGAQTSTIG-GSDWAIAISANGKKKEAAVKFLKYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 348 AdDKEWGPKNVVRTGAFPVRTSYGDLYKDKRMEKIAEWTKFYSPYYNT--IDGFAE-MRTLWFPMVQAISNGDEKPEDAL 424
Cdd:cd14749 301 T-SPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTpfLDEYWPaAAQVHKDAVQKLLTGKIDPEQVV 379
|
....*....
gi 1611951076 425 KAFTEKANK 433
Cdd:cd14749 380 KQAQSAAAK 388
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
41-436 |
2.82e-22 |
|
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: 97.77 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 41 EITWWAFPVFTQEKAEdgvgtyeKKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNG 120
Cdd:cd14747 1 TLTVWAMGNSAEAELL-------KELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 121 KLADLNDLFTKEFTKDVNNDKLIQASKAGDTAYMYPI---SSAPFYmalNKKMLKDAGVLDLVKegwTTDDFEKVLKALK 197
Cdd:cd14747 74 ALEDLTPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWyadTRALFY---RTDLLKKAGGDEAPK---TWDELEAAAKKIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 198 DKGynpGSFFANG-QGGDQGPRAFFANLYS---SHITDDKvTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDGSADIQ 273
Cdd:cd14747 148 ADG---PDVSGFAiPGKNDVWHNALPFVWGaggDLATKDK-WKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 274 NFANGQTSFtILWAPAQPGI--QAKLLEASKVDYLEIPFPSDDGKPeleylvnGF------AVFnnKDEQKVAASKTFIQ 345
Cdd:cd14747 224 AFANGKVAM-IISGPWEIGAirEAGPDLAGKWGVAPLPGGPGGGSP-------SFaggsnlAVF--KGSKNKDLAWKFIE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 346 FIAddkewGPKNVVR----TGAFPVRTSYGD---LYKDKRMEKIAE---WTKFY--SPYYNTIDgfAEMRTLWFpmvQAI 413
Cdd:cd14747 294 FLS-----SPENQAAyakaTGMLPANTSAWDdpsLANDPLLAVFAEqlkTGKATpaTPEWGEIE--AELVLVLE---EVW 363
|
410 420
....*....|....*....|...
gi 1611951076 414 SNGDEKPEDALKAFTEKANKTIK 436
Cdd:cd14747 364 IGVGADVEDALDKAAAEINEILN 386
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
64-435 |
8.22e-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: 90.43 E-value: 8.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 64 KKLIAAFEKANPeIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDLFTKEFTkdvNNDKLI 143
Cdd:cd13586 16 KELAEEFEKKYG-IKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIK---NLPVAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 144 QASKAGDTAYMYPISSAPFYMALNKKMLKDAgvldlVKegwTTDDFEKVLKALKDKG-------YNPGSF-----FANGQ 211
Cdd:cd13586 92 AAVTYNGKLYGVPVSVETIALFYNKDLVPEP-----PK---TWEELIALAKKFNDKAggkygfaYDQTNPyfsypFLAAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 212 GGdqgpRAFFANlysshitDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDGSADiQNFANGQTSFTI--LWApa 289
Cdd:cd13586 164 GG----YVFGEN-------GGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIAD-ALFKEGKAAMIIngPWD-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 290 qpgiqAKLLEASKVDYLEIPFPSDDGKPELEYLVNGFAVFNNKDEQKVAASKTFIQFIADDKEwGPKNVVRTGAFPVRTS 369
Cdd:cd13586 230 -----LADYKDAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEA-QLLLFEKTGRIPALKD 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1611951076 370 Y---GDLYKDKRMEKIAEWTKFYSPYYNTidgfAEMRTLWFPMVQAISN---GDEKPEDALKafteKANKTI 435
Cdd:cd13586 304 AlndAAVKNDPLVKAFAEQAQYGVPMPNI----PEMAAVWDAMGNALNLvasGKATPEEAAK----DAVAAI 367
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
64-351 |
1.11e-19 |
|
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: 89.01 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 64 KKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAP-DVLFDAPGRIIQYGKNGKLADLNDLFTKEFTKDVNndkl 142
Cdd:pfam01547 11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 143 iqaskagdTAYMYPISSAPFYMALNKKMLKDAGvldlVKEGWTTDDFEKVLKALKDKGYNPG--SFFANGQGGDQGPRAF 220
Cdd:pfam01547 87 --------KLYGVPLAAETLGLIYNKDLFKKAG----LDPPKTWDELLEAAKKLKEKGKSPGgaGGGDASGTLGYFTLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 221 FANLYSSHITDDKVTKYTTDDANSIKAMTK---ISNWIKDGLMMNGSQYDGSADIQNFANGQTSFTILW-----APAQPG 292
Cdd:pfam01547 155 LASLGGPLFDKDGGGLDNPEAVDAITYYVDlyaKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGpwaalAANKVK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1611951076 293 IQAKLLEASKVDYLEIPFPSDDGKPELEYLVNGFAVFNNKDEQKVAasKTFIQFIADDK 351
Cdd:pfam01547 235 LKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAA--KKFLDFLTSPE 291
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
65-350 |
1.39e-17 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 82.45 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 65 KLIAAFEKANPeIKVKLETIDFTSGPEKITTAIEAGTAPD--VLFDAPGRIIQYGKNGKLADLNDLFTKEFTKDVNNDkl 142
Cdd:pfam13416 1 ALAKAFEKKTG-VTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 143 iqASKAGDTAYMYPISSAPFYMALNKKMLKDAGvldlvKEGWTTDDFEKVLKALKDK--GYNPGSFFangqggdqgpraF 220
Cdd:pfam13416 78 --AGYDGKLYGVPYAASTPTVLYYNKDLLKKAG-----EDPKTWDELLAAAAKLKGKtgLTDPATGW------------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 221 FANLYSSHITDDKVTKYTTDdanSIKAMTKISNWIKDGLMMNgsqyDGSADIQNFANGQTSFTILWAPAQPGIQAkllEA 300
Cdd:pfam13416 139 LWALLADGVDLTDDGKGVEA---LDEALAYLKKLKDNGKVYN----TGADAVQLFANGEVAMTVNGTWAAAAAKK---AG 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1611951076 301 SKVDYLeipFPsddgKPELEYLVNGFAVFNNKDEQKVAAsKTFIQFIADD 350
Cdd:pfam13416 209 KKLGAV---VP----KDGSFLGGKGLVVPAGAKDPRLAA-LDFIKFLTSP 250
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
64-431 |
1.98e-17 |
|
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: 83.23 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 64 KKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDLFTKeftKDVNNDKLI 143
Cdd:cd13522 17 NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSK---SGKYAPNTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 144 QASKAGDTAYMYPISSAPFYMALNKKMLKDagvldlvKEGWTTDDFEKVLKALKDKG-------YNPGSFFANGQGGDQG 216
Cdd:cd13522 94 AAMKLNGKLYGVPVSVGAHLMYYNKKLVPK-------NPPKTWQELIALAQGLKAKNvwglvynQNEPYFFAAWIGGFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 217 prAFFAnlysshiTDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDGSADiQNFANGQTSFTILWapaqPGIQAK 296
Cdd:cd13522 167 --QVFK-------ANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIAD-ALFKAGKAAMIING----PWDLGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 297 LLEASKVDYLEIPFPSDDGKPELEYLVNGFAVFNNKDEQKVAASKTFIQFIADDKEwGPKNVVRTGAFPVRTS-YGDLYK 375
Cdd:cd13522 233 YRQALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQA-QLVLFDDAGDIPANLQaYESPAV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1611951076 376 DKR--MEKIAEWTKFYSPYYNTidgfAEMRTLWFPM---VQAISNGDEKPEDALKAFTEKA 431
Cdd:cd13522 312 QNKpaQKASAEQAAYGVPMPNI----PEMRAVWDAFriaVNSVLAGKVTPEAAAKDAQQEA 368
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
41-430 |
3.65e-16 |
|
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: 79.65 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 41 EITWWAFPVFTQEKaedgvgtYEKKLIAAFEKANPEIKVKLETIDFTSGP--EKITTAIEAG-TAPDVL-FDAPgRIIQY 116
Cdd:cd14750 1 TITFAAGSDGQEGE-------LLKKAIAAFEKKHPDIKVEIEELPASSDDqrQQLVTALAAGsSAPDVLgLDVI-WIPEF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 117 GKNGKLADLndlfTKEFTKDVNNDKL---IQASKAGDTAYmypisSAPFYMalnkkmlkDAGVL----DLVKEGW----- 184
Cdd:cd14750 73 AEAGWLLPL----TEYLKEEEDDDFLpatVEANTYDGKLY-----ALPWFT--------DAGLLyyrkDLLEKYGpeppk 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 185 TTDDFEKVLKALKDKGYNPGSFFANGQGGDQGPRAFFANLYSS--HITDDKVTKYTTDDANSIKAMTKISNWIKDGLMMN 262
Cdd:cd14750 136 TWDELLEAAKKRKAGEPGIWGYVFQGKQYEGLVCNFLELLWSNggDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 263 GSQYDGSADIQN-FANGQTSFTILWAPAQPGIQAKLLE-ASKVDYLEIP-FPSDDGKPELEylvnGFAVFNNKDEQKVAA 339
Cdd:cd14750 216 GVLTYGEEEARAaFQAGKAAFMRNWPYAYALLQGPESAvAGKVGVAPLPaGPGGGSASTLG----GWNLAISANSKHKEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 340 SKTFIQFIAdDKEWGPKNVVRTGAFPVRtsyGDLYKDKRM-EKIAEWTKFY-----------SPYYNtidgfaEMRTLWF 407
Cdd:cd14750 292 AWEFVKFLT-SPEVQKRRAINGGLPPTR---RALYDDPEVlEAYPFLPALLealenavprpvTPKYP------EVSTAIQ 361
|
410 420
....*....|....*....|...
gi 1611951076 408 PMVQAISNGDEKPEDALKAFTEK 430
Cdd:cd14750 362 IALSAALSGQATPEEALKQAQEK 384
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
42-426 |
2.18e-15 |
|
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: 77.42 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 42 ITWWAfpvfTQEKAEdgvGTYEKKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGK 121
Cdd:cd14751 2 ITFWH----TSSDEE---KVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 122 LADLNDLFTKEFTKDVNNDKLIQASKAGDTaYMYPISS---APFYmalNKKMLKDAGV---------LDLVKEGWTTDDf 189
Cdd:cd14751 75 LQPLDGTPAFDDIVDYLPGPMETNRYNGHY-YGVPQVTntlALFY---NKRLLEEAGTevpktmdelVAAAKAIKKKKG- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 190 EKVLKALKDKGYNPGSFFaNGQGGDqgpraffanlysshITDDKVTKYTTDDANSIKAMTKISNWIKDGLMMnGSQYDGS 269
Cdd:cd14751 150 RYGLYISGDGPYWLLPFL-WSFGGD--------------LTDEKKATGYLNSPESVRALETIVDLYDEGAIT-PCASGGY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 270 ADIQN-FANGQTSFtILWAPAQPGIQAKLLEASKVDYLEI-PFPsddGKPELEYLVNG---FAVFNNKDEQKvaASKTFI 344
Cdd:cd14751 214 PNMQDgFKSGRYAM-IVNGPWAYADILGGKEFKDPDNLGIaPVP---AGPGGSGSPVGgedLVIFKGSKNKD--AAWKFV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 345 QFIADDKEwGPKNVVRTGAFPVRTSygdLYKDKRMEKIAEwTKFYSPYYNT------IDGFAEMRTLWFPMVQAISNGDE 418
Cdd:cd14751 288 KFMSSAEA-QALTAAKLGLLPTRTS---AYESPEVANNPM-VAAFKPALETavprppIPEWGELFEPLTLAFAKVLRGEK 362
|
....*...
gi 1611951076 419 KPEDALKA 426
Cdd:cd14751 363 SPREALDE 370
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
62-425 |
4.45e-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: 73.29 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 62 YEKKLIAAFEKANpEIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDLFTKeftKDVNNDK 141
Cdd:cd13658 14 FIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSKDK---KKGFTDQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 142 LIQASKAGDTAYMYPISSAPFYMALNKKMLKDA-----GVLDLVKEgwTTDDFEK---VLKALKDKGYNPGSFFANGqgg 213
Cdd:cd13658 90 ALKALTYDGKLYGLPAAVETLALYYNKDLVKNApktfdELEALAKD--LTKEKGKqygFLADATNFYYSYGLLAGNG--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 214 dqgpraffANLYSSHITDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGSQYDgsADIQNFANGQTSFTI--LWApaqp 291
Cdd:cd13658 165 --------GYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD--VIQGLFKEGKAAAVIdgPWA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 292 giqAKLLEASKVDYLEIPFPSDDGKPELEYLVNGFAVFNNKDEQKVAASKTFIQFIAdDKEWGPKNVVRTGAFPVRT--- 368
Cdd:cd13658 231 ---IQEYQEAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLT-SKENLKKRYDETNEIPPRKdvr 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 369 SYGDLYKDKRMEKIAEWTKFYSPYYNtidgFAEMRTLWFPMVQA---ISNGDEKPEDALK 425
Cdd:cd13658 307 SDPEIKNNPLTSAFAKQASRAVPMPN----IPEMGAVWEPANNAlffILSGKKTPKQALN 362
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
64-426 |
3.84e-12 |
|
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: 67.40 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 64 KKLIAAFEKANPEIKVKletIDFTSGPE---KITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDlftkEFTKDVNND 140
Cdd:cd13657 17 QQIIDEFEAKYPVPNVK---VPFEKKPDlqnKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISD----YLSEDDFEN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 141 KLIQASKAG---DTAYMYPISSAPFYMALNKKMLKDAGVldlvkegwTTDDFEKVLKALKDKgyNPGSFFANGQGGDQGP 217
Cdd:cd13657 90 YLPTAVEAVtykGKVYGLPEAYETVALIYNKALVDQPPE--------TTDELLAIMKDHTDP--AAGSYGLAYQVSDAYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 218 RAFFANLYSSHITDDKVTKYTTDDANSIKAMTKISNWIKDGLmmngsQYDGSADIQN--FANGQTSFTIL--WAPAQpgi 293
Cdd:cd13657 160 VSAWIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPYM-----PSDPSYNTQTslFNEGKAAMIINgpWFIGG--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 294 qaklLEASKVDYLEIPFPS-DDGKPELEYL-VNGFAVFNNKDEQKVAASKTFIQFIADDkEWGPKNVVRTGAFPVRTsyg 371
Cdd:cd13657 232 ----IKAAGIDLGVAPLPTvDGTNPPRPYSgVEGIYVTKYAERKNKEAALDFAKFFTTA-EASKILADENGYVPAAT--- 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1611951076 372 DLYKDKRMEKIAEWTKFYS------PYYNTidgfAEMRTLWFPM---VQAISNGDEKPEDALKA 426
Cdd:cd13657 304 NAYDDAEVAADPVIAAFKAqaehgvPMPNS----PEMASVWGPVtlaLAAVYQGGQDPQEALAA 363
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
39-350 |
1.15e-09 |
|
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: 60.03 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 39 KTEITWWAFPVFTQ-EKAEDGVGT--YEKKLiaafekanpEIKVKLETIDFTSGPEKITTAIEAGTAPDVLF-DAPGRII 114
Cdd:cd13580 2 PVTITIVANLGGNPkPDPDDNPYTkyLEEKT---------NIDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 115 QYGKNGKLADLNDLFTK---EFTKDVNNDKLIQASKAGDtayMYPI-----SSAPFYMALNKKMLKDAGvLDLVKegwTT 186
Cdd:cd13580 73 TLVKQGALWDLTDYLDKyypNLKKIIEQEGWDSASVDGK---IYGIprkrpLIGRNGLWIRKDWLDKLG-LEVPK---TL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 187 DDFEKVLKALKDK-----GYNPGSFFANGQGGDQGPRAFFANLYSSHITDDKVTK-----YTTDDANSIKAMTKISNWIK 256
Cdd:cd13580 146 DELYEVAKAFTEKdpdgnGKKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWWKDEdgklvPGSIQPEMKEALKFLKKLYK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 257 DGLM------MNGSQYDgsadiQNFANGQTSFTI--LWAPAQPGIQAKlLEASKVDYLEIPFPS-DDGK--PELEYLVNG 325
Cdd:cd13580 226 EGLIdpefavNDGTKAN-----EKFISGKAGIFVgnWWDPAWPQASLK-KNDPDAEWVAVPIPSgPDGKygVWAESGVNG 299
|
330 340
....*....|....*....|....*
gi 1611951076 326 FAVFnNKDEQKVAASKTFIQFIADD 350
Cdd:cd13580 300 FFVI-PKKSKKPEAILKLLDFLSDP 323
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
63-347 |
9.99e-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: 270301 [Multi-domain] Cd Length: 478 Bit Score: 53.90 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 63 EKKLIAAFEKANPEIKVKLETIDFTSGPEKITTAIEAGTAPD---VLFdaPGRIIQYGKNGKLADLNDLFT-----KEFT 134
Cdd:cd13583 18 DDWLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDiipVLY--PGEENEFVASGALLPISDYLDympnyKKYV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 135 KDVNNDKLIQASKAGDTA-YMYP---ISSAPFYMAL-NKKMLKDAGVldlvKEGWTTDDFEKVLKALKDKGynPGSFFAN 209
Cdd:cd13583 96 EKWGLGKELATGRQSDGKyYSLPglhEDPGVQYSFLyRKDIFEKAGI----KIPTTWDEFYAALKKLKEKY--PDSYPYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 210 GQGGDQGPRAFFANLYSSHI-----------TDDKVTKYTTDDaNSIKAMTKISNWIKDGLMMNGSQYDGSADI-QNFAN 277
Cdd:cd13583 170 DRWNSNALLLIAAPAFGTTAgwgfsnytydpDTDKFVYGATTD-EYKDMLQYFNKLYAEGLLDPESFTQTDDQAkAKFLN 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1611951076 278 GQTSFTILWAPAQPGIQAKLLEASKVDYLEIPFPSDDGKP----ELEYLVNGFAVF-NNKDEQKVAASKTFIQFI 347
Cdd:cd13583 249 GKSFVITTNPQTVDELQRNLRAADGGNYEVVSITPPAGPAgkaiNGSRLENGFMISsKAKDSKNFEALLQFLDWL 323
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
71-290 |
1.37e-07 |
|
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: 270299 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 71 EKANpeIKVKLETIDFTSGPEKITTAIEAGTAPDVLFDA---PGRIIQYGKNGKLADLNDLFTKEFT--KDVNNDKLiqA 145
Cdd:cd13581 28 EKTG--IKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAgasDADLMTYGKQGLFLPLEDLIDKYAPnlKALFDENP--D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 146 SKAGDTA-----YMYP------ISSAPFYMALNKKMLKDAGvLDLVKegwTTDDFEKVLKALKDKGYN--------PGSF 206
Cdd:cd13581 104 IKAAITApdghiYALPsvnecyHCSYGQRMWINKKWLDKLG-LEMPT---TTDELYEVLKAFKEQDPNgngkadeiPLSF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 207 FANGqGGDQGPRAFFA------NLYSSH--ITDDKVTKYTTDDANSIKAMTKISNWIKDGLMMNGS---QYDGSADIQNF 275
Cdd:cd13581 180 SGLN-GGTDDPAFLLNsfgindGGYGGYgfVVKDGKVIYTATDPEYKEALAYLNKLYKEGLIDPEAftqDYDQLAAKGKA 258
|
250
....*....|....*
gi 1611951076 276 ANGQTSFTILWAPAQ 290
Cdd:cd13581 259 STAKVGVFFGWDPGL 273
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
77-426 |
1.97e-06 |
|
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: 49.52 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 77 IKVKLETIDftSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDlfTKEFTKDVNNdKLIQASKAGDTAYMYP 156
Cdd:cd13656 29 IKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP--DKAFQDKLYP-FTWDAVRYNGKLIAYP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 157 ISSAPFYMALNKKMLKDAGVldlvkegwTTDDFEKVLKALKDKGYNP------GSFFANGQGGDQGPRAFFANLYSSHIT 230
Cdd:cd13656 104 IAVEALSLIYNKDLLPNPPK--------TWEEIPALDKELKAKGKSAlmfnlqEPYFTWPLIAADGGYAFKYENGKYDIK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 231 DDKVtkyttDDANSIKAMTKISNWIKDGLMMNGSQYdgSADIQNFANGQTSFTIL--WAPAQpgiqaklLEASKVDYLEI 308
Cdd:cd13656 176 DVGV-----DNAGAKAGLTFLVDLIKNKHMNADTDY--SIAEAAFNKGETAMTINgpWAWSN-------IDTSKVNYGVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 309 PFPSDDGKPELEYLVNGFAVFNNKDEQKVAASKTFIQFIADDKewGPKNV---VRTGAFPVRTSYGDLYKDKRMEKIAEW 385
Cdd:cd13656 242 VLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDE--GLEAVnkdKPLGAVALKSYEEELAKDPRIAATMEN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1611951076 386 TKFYSPYYNtidgFAEMRTLWFPM---VQAISNGDEKPEDALKA 426
Cdd:cd13656 320 AQKGEIMPN----IPQMSAFWYAVrtaVINAASGRQTVDEALKD 359
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
91-287 |
7.62e-05 |
|
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain] Cd Length: 481 Bit Score: 44.74 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 91 EKITTAIEAGTAPDVL----FDAPGRIIQYGKNGKLADLNDL-------FTKEFTKDVNNDKLIQASkAGDTAYMYPISS 159
Cdd:cd13584 47 EQFNLMMASGQLPDIIggdwLKDKGGFEKYGEDGAFLPLNDLidqyapnLKKFLDEHPDVKKAITTD-DGNIYGFPYLPD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 160 ApfymalnkKMLKDAGVLdLVKEGW----------TTDDFEKVLKALKDKGYNPGS------FFANGQGGDQgpRAFFAN 223
Cdd:cd13584 126 G--------DVAKEARGY-FIRKDWldklglktpsTIDEWYTVLKAFKERDPNGNGkadevpLILTKPGYDE--TGRLIN 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1611951076 224 L---YSSHITDDKVTKYTTDDANSIKAMTKISNWIKDGLM-MNGSQYDGSADIQNFANGQT-SFTILWA 287
Cdd:cd13584 195 AwgaYMDFYQENGKVKYGPLEPGFKDFLKTMNQWYKEGLIdPDFFTRKAKAREQNIMNGNIgGFTHDWF 263
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-317 |
1.04e-04 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 44.23 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 1 MNMKKFASLAMLGAsVLGLAACGGKSQKeasesksdAAKTEITWWafpvFTQEKAEDGVGTYEKKliaaFEKANpEIKVK 80
Cdd:PRK09474 1 MKIKKGLRTLALSA-LATLMFSASALAK--------IEEGKLVIW----INGDKGYNGLAEVGKK----FEKDT-GIKVT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 81 LETIDftSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLADLNDlfTKEFtKDVNNDKLIQASKAGDTAYMYPISSA 160
Cdd:PRK09474 63 VEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTP--SKAF-KDKLVPFTWDAVRYNGKLIGYPIAVE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 161 PFYMALNKkmlkdagvlDLVKEGWTT-DDFEKVLKALKDKG-------YNPGSF---FANGQGGdqgpraffanlYSSHI 229
Cdd:PRK09474 138 ALSLIYNK---------DLVPTPPKTwEEIPALDKELKAKGksaimwnLQEPYFtwpLIAADGG-----------YAFKF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 230 TDdkvTKYTTDD-----ANSIKAMTKISNWIKDGLMMNGSQYdGSADIQnFANGQTSFTI--LWAPAQpgiqaklLEASK 302
Cdd:PRK09474 198 EN---GGYDVKDvgvnnAGAKAGLQFLVDLVKNKHMNADTDY-SIAEAA-FNKGETAMTIngPWAWSN-------IDKSG 265
|
330
....*....|....*
gi 1611951076 303 VDYLEIPFPSDDGKP 317
Cdd:PRK09474 266 INYGVTVLPTFNGKP 280
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
64-210 |
2.00e-03 |
|
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 40.02 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 64 KKLIAAFEKANPEIKvkletIDFTSGPEKITTAIE-----AGTAPDVLFDAPGRIIQYGKNGKLADLNDlFTKEFTKDVN 138
Cdd:cd13655 15 KEMVDAFKEKHPEWK-----ITITIGVVGEADAKDevlkdPSAAADVFAFANDQLGELVDAGAIYPLTG-SAVDKIKNTN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1611951076 139 NDKLIQASKAGDTAYMYPISSAPFYMALNKKMLKDagvlDLVKegwttdDFEKVLKALKDKGYNPGSFFANG 210
Cdd:cd13655 89 SEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTE----DDVK------SLDTMLAKAPDAKGKVSFDLSNS 150
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1-174 |
4.00e-03 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 39.12 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 1 MNMKKFASLAMLGASVLGLAAcggksqkeaseSKSDAAKTEITWWAFPvftqekaedgvGTYEKKLIAAFEKANpEIKVK 80
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGG-----------APAAAAEGTLNVYNWG-----------GYIDPDVLEPFEKET-GIKVV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1611951076 81 LETIDftsGPEKITTAIEAGTAP-DVLFDAPGRIIQYGKNGKLADLNdlftkeFTKDVN----NDKLIQASKAGDTAYMY 155
Cdd:COG0687 58 YDTYD---SNEEMLAKLRAGGSGyDVVVPSDYFVARLIKAGLLQPLD------KSKLPNlanlDPRFKDPPFDPGNVYGV 128
|
170
....*....|....*....
gi 1611951076 156 PISSAPFYMALNKKMLKDA 174
Cdd:COG0687 129 PYTWGTTGIAYNTDKVKEP 147
|
|
| |
