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Conserved domains on  [gi|736880152|ref|WP_034879743|]
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MULTISPECIES: extracellular solute-binding protein [Bifidobacterium]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 51-428 7.79e-106

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd14747:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 386  Bit Score: 318.49  E-value: 7.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGN--EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNS--FSTVPDN 126
Cdd:cd14747    2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMgaLEDLTPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 127 L----DMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGWNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSs 202
Cdd:cd14747   82 LedlgGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAIPG- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 203 GTDAFLGTLPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAV 282
Cdd:cd14747  161 KNDVWHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 283 SQINELGGDGfESKYATVILPSMNESSGPatSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKA 362
Cdd:cd14747  241 GAIREAGPDL-AGKWGVAPLPGGPGGGSP--SFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSA 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736880152 363 WDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKG-QVSVDEGLKNLQSEADSI 428
Cdd:cd14747  318 WDDPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAAEINEI 384
 
Name Accession Description Interval E-value
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 51-428 7.79e-106

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: 318.49  E-value: 7.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGN--EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNS--FSTVPDN 126
Cdd:cd14747    2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMgaLEDLTPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 127 L----DMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGWNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSs 202
Cdd:cd14747   82 LedlgGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAIPG- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 203 GTDAFLGTLPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAV 282
Cdd:cd14747  161 KNDVWHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 283 SQINELGGDGfESKYATVILPSMNESSGPatSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKA 362
Cdd:cd14747  241 GAIREAGPDL-AGKWGVAPLPGGPGGGSP--SFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSA 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736880152 363 WDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKG-QVSVDEGLKNLQSEADSI 428
Cdd:cd14747  318 WDDPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAAEINEI 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
2-428 6.37e-83

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 260.27  E-value: 6.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152   2 MKSffKASVATVVSAVMVIGMSSCGRSESGADSDSdavktinSSKATGDLTIWAMGNEGDLLDDFVKGFEKEnPDVKIKV 81
Cdd:COG2182    1 MKR--RLLAALALALALALALAACGSGSSSSGSSS-------AAGAGGTLTVWVDDDEAEALEEAAAAFEEE-PGIKVKV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  82 TAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADF--SNSFSTVPDNLDM-SDFSDGSRATGQVDGKQLGVPWYIDTRVL 158
Cdd:COG2182   71 VEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELaeAGLLAPLDDDLADkDDFLPAALDAVTYDGKLYGVPYAVETLAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 159 YYRTDIAGmagwNKAPKTWNELKRMAKDMQKVDgvKYGMSLNssGTDAFLgTLPFSYSAGASLTNEEQ---TKWTFDDNG 235
Cdd:COG2182  151 YYNKDLVK----AEPPKTWDELIAAAKKLTAAG--KYGLAYD--AGDAYY-FYPFLAAFGGYLFGKDGddpKDVGLNSPG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 236 IKKGLNFTTSLYRDGIVDVNADVSSGadIANFVSGSTPMMLQGPTAVSQINELGGDgfesKYATVILPSMNESsGPATSF 315
Cdd:COG2182  222 AVAALEYLKDLIKDGVLPADADYDAA--DALFAEGKAAMIINGPWAAADLKKALGI----DYGVAPLPTLAGG-KPAKPF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 316 VGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQ 395
Cdd:COG2182  295 VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGA 374

                        410       420       430
                 ....*....|....*....|....*....|...
gi 736880152 396 VSSVADRILEQINKGQVSVDEGLKNLQSEADSI 428
Cdd:COG2182  375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 59-347 6.14e-30

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: 117.52  E-value: 6.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152   59 EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGP-DLAQMGTTWMADFSNsfSTVPDNLDmsdfSDGSR 137
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK--AGLLLPLD----DYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  138 ATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGwNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSSGTDAFLGTLPFSYSA 217
Cdd:pfam01547  80 YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAG-LDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLASL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  218 GASLTNEEQ----TKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAVSQIN--ELGGD 291
Cdd:pfam01547 159 GGPLFDKDGggldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANkvKLKVA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 736880152  292 GFESKYATVILPSMNESSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQA 347
Cdd:pfam01547 239 FAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
49-338 3.21e-12

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 67.73  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  49 GDLTIWAMGNEG-DLLDDFVKGFEKenpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDL-----------AQMG----TTW 112
Cdd:PRK09474  31 GKLVIWINGDKGyNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDIifwahdrfggyAQSGllaeVTP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 113 MADFSNSFStvpdnldmsDFS-DGSRatgqVDGKQLGVPWYIDTRVLYYRTDIAgmagwNKAPKTWNELKRMAKDMQKvD 191
Cdd:PRK09474 108 SKAFKDKLV---------PFTwDAVR----YNGKLIGYPIAVEALSLIYNKDLV-----PTPPKTWEEIPALDKELKA-K 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 192 GvKYGMSLNSSGTdAFlgTLPFSYSAGASLTNEEQTKWTFDDNGI-----KKGLNFTTSLYRDGIVDVNADVSSGAdiAN 266
Cdd:PRK09474 169 G-KSAIMWNLQEP-YF--TWPLIAADGGYAFKFENGGYDVKDVGVnnagaKAGLQFLVDLVKNKHMNADTDYSIAE--AA 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736880152 267 FVSGSTPMMLQGPTAVSQINELGGDgfeskYATVILPSMNesSGPATSFVG----GCNLVtfkdSKNKQSAWKFIQ 338
Cdd:PRK09474 243 FNKGETAMTINGPWAWSNIDKSGIN-----YGVTVLPTFN--GKPSKPFVGvlsaGINAA----SPNKELAKEFLE 307
 
Name Accession Description Interval E-value
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 51-428 7.79e-106

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: 318.49  E-value: 7.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGN--EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNS--FSTVPDN 126
Cdd:cd14747    2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMgaLEDLTPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 127 L----DMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGWNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSs 202
Cdd:cd14747   82 LedlgGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAIPG- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 203 GTDAFLGTLPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAV 282
Cdd:cd14747  161 KNDVWHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 283 SQINELGGDGfESKYATVILPSMNESSGPatSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKA 362
Cdd:cd14747  241 GAIREAGPDL-AGKWGVAPLPGGPGGGSP--SFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSA 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736880152 363 WDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKG-QVSVDEGLKNLQSEADSI 428
Cdd:cd14747  318 WDDPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAAEINEI 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
2-428 6.37e-83

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 260.27  E-value: 6.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152   2 MKSffKASVATVVSAVMVIGMSSCGRSESGADSDSdavktinSSKATGDLTIWAMGNEGDLLDDFVKGFEKEnPDVKIKV 81
Cdd:COG2182    1 MKR--RLLAALALALALALALAACGSGSSSSGSSS-------AAGAGGTLTVWVDDDEAEALEEAAAAFEEE-PGIKVKV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  82 TAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADF--SNSFSTVPDNLDM-SDFSDGSRATGQVDGKQLGVPWYIDTRVL 158
Cdd:COG2182   71 VEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELaeAGLLAPLDDDLADkDDFLPAALDAVTYDGKLYGVPYAVETLAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 159 YYRTDIAGmagwNKAPKTWNELKRMAKDMQKVDgvKYGMSLNssGTDAFLgTLPFSYSAGASLTNEEQ---TKWTFDDNG 235
Cdd:COG2182  151 YYNKDLVK----AEPPKTWDELIAAAKKLTAAG--KYGLAYD--AGDAYY-FYPFLAAFGGYLFGKDGddpKDVGLNSPG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 236 IKKGLNFTTSLYRDGIVDVNADVSSGadIANFVSGSTPMMLQGPTAVSQINELGGDgfesKYATVILPSMNESsGPATSF 315
Cdd:COG2182  222 AVAALEYLKDLIKDGVLPADADYDAA--DALFAEGKAAMIINGPWAAADLKKALGI----DYGVAPLPTLAGG-KPAKPF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 316 VGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQ 395
Cdd:COG2182  295 VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGA 374

                        410       420       430
                 ....*....|....*....|....*....|...
gi 736880152 396 VSSVADRILEQINKGQVSVDEGLKNLQSEADSI 428
Cdd:COG2182  375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 51-425 7.01e-77

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: 243.85  E-value: 7.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGN--EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNSFSTVP---- 124
Cdd:cd13585    2 LTFWDWGQpaETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDlddy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 125 --DNLDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDI---AGMAgwNKAPKTWNELKRMAKDMQKVDGVKYGMSL 199
Cdd:cd13585   82 ieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLfdkAGPG--PKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 200 NSSGTDAFlGTLPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGP 279
Cdd:cd13585  160 RGGSGGQT-QWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMIDGP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 280 TAVSQINELGGDGfesKYATVILPSMneSSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPAS 359
Cdd:cd13585  239 WALGTLKDSKVKF---KWGVAPLPAG--PGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALA 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 360 QKAWDEDALSGNDKLA--AFGDQLKNTMAPPALSTWAQVSSVADRILEQI--NKGQVSVDEGLKNLQSEA 425
Cdd:cd13585  314 AAAASAAAPDAKPALAlaAAADALAAAVPPPVPPPWPEVYPILSEALQEAllGALGKSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 11-349 4.77e-75

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 238.41  E-value: 4.77e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  11 ATVVSAVMVIGMSSCGRSESGADSDSDAVKtinsskatgdLTIWAM-GNEGDLLDDFVKGFEKENPDVKIKVTAIPWSSA 89
Cdd:COG1653    5 ALALAAALALALAACGGGGSGAAAAAGKVT----------LTVWHTgGGEAAALEALIKEFEAEHPGIKVEVESVPYDDY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  90 HDKLQTAIAAGNGPDLAQMGTTWMADFSNSFSTVP-------DNLDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRT 162
Cdd:COG1653   75 RTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPlddllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 163 DIAGMAGWnKAPKTWNELKRMAKDMQKVDGVkYGMSLNSSGTDAFlgtLPFSYSAGASLTNEEqTKWTFDDNGIKKGLNF 242
Cdd:COG1653  155 DLFEKAGL-DPPKTWDELLAAAKKLKAKDGV-YGFALGGKDGAAW---LDLLLSAGGDLYDED-GKPAFDSPEAVEALEF 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 243 TTSLYRDGIVDVNADVSSGAD-IANFVSGSTPMMLQGPTAVSQINELGGDgfeSKYATVILPSMnESSGPATSFVGGCNL 321
Cdd:COG1653  229 LKDLVKDGYVPPGALGTDWDDaRAAFASGKAAMMINGSWALGALKDAAPD---FDVGVAPLPGG-PGGKKPASVLGGSGL 304

                        330       340
                 ....*....|....*....|....*...
gi 736880152 322 VTFKDSKNKQSAWKFIQWASKPEVQAEW 349
Cdd:COG1653  305 AIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 51-425 3.01e-74

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: 237.19  E-value: 3.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAM--GNEGDLLDDFVKGFEKENPDVKIKVTAIPWSS-AHDKLQTAIAAGNGPDLAQMGTTWMADFSNSFSTVP--- 124
Cdd:cd14748    2 ITFWHGmsGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPldd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 125 ----DNLDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDI---AGMAGwNKAPKTWNELKRMAK--DMQKVDGVKY 195
Cdd:cd14748   82 yidkDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLfeeAGLDP-EKPPKTWDELEEAAKklKDKGGKTGRY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 196 GMSLNSSGTDAFLGTlpFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLY-RDGIVDVNADVSSGADianFVSGSTPM 274
Cdd:cd14748  161 GFALPPGDGGWTFQA--LLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVgKDGVSPLNDWGDAQDA---FISGKVAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 275 MLQGPTAVSQINElGGDGFEskYATVILPSmnESSGPATSFVGGCNLVTFKD-SKNKQSAWKFIQWASKPEVQAEWYKKS 353
Cdd:cd14748  236 TINGTWSLAGIRD-KGAGFE--YGVAPLPA--GKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKAT 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736880152 354 SDLPASQKAWD--EDALSGNDKLAAFGDQLKNTMA-PPALSTWAQVSSVADRILEQINKGQVSVDEGLKNLQSEA 425
Cdd:cd14748  311 GYLPVRKSAAEdpEEFLAENPNYKVAVDQLDYAKPwGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 51-426 6.35e-63

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: 207.62  E-value: 6.35e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGN--EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNSFSTVP-DNL 127
Cdd:cd14751    2 ITFWHTSSdeEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPlDGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 128 ----DMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGwNKAPKTWNELKRMAKDMQKVDGvKYGMSLNssG 203
Cdd:cd14751   82 pafdDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAG-TEVPKTMDELVAAAKAIKKKKG-RYGLYIS--G 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 204 TDAFlGTLPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAVS 283
Cdd:cd14751  158 DGPY-WLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAITPCASGGYPNMQDGFKSGRYAMIVNGPWAYA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 284 QIneLGGDGFESKYATVILPsMNESSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKAW 363
Cdd:cd14751  237 DI--LGGKEFKDPDNLGIAP-VPAGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAY 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736880152 364 DEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQVSVDEGLKNLQSEAD 426
Cdd:cd14751  314 ESPEVANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 57-424 1.39e-54

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: 185.96  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  57 GNEGDLLDDFVKGFEKENPDVKIKVTAIPWSS--AHDKLQTAIAAGN-GPDLAQMGTTWMADFSNSFSTVPDNLDMS--- 130
Cdd:cd14750   10 GQEGELLKKAIAAFEKKHPDIKVEIEELPASSddQRQQLVTALAAGSsAPDVLGLDVIWIPEFAEAGWLLPLTEYLKeee 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 131 --DFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGwNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSSGTDAFL 208
Cdd:cd14750   90 ddDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYG-PEPPKTWDELLEAAKKRKAGEPGIWGYVFQGKQYEGLV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 209 GT-LPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIAN-FVSGSTPMMLQGPTAVSqin 286
Cdd:cd14750  169 CNfLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARAaFQAGKAAFMRNWPYAYA--- 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 287 elGGDGFESKYATVI----LPSMNEssGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQKA 362
Cdd:cd14750  246 --LLQGPESAVAGKVgvapLPAGPG--GGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPPTRRAL 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736880152 363 WDEDALSGNDK-LAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQVSVDEGLKNLQSE 424
Cdd:cd14750  322 YDDPEVLEAYPfLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEK 384
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 50-427 4.12e-45

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: 161.01  E-value: 4.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  50 DLTIWAMGNEGD---LLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQM-GTTWMADF--SNSFSTV 123
Cdd:cd14749    1 TITYWQYFTGDTkkkYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFvkAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 124 PDNLDMSD----FSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGWNKAPKTWNELKRMAKDMQKVDGVKYGMSL 199
Cdd:cd14749   81 TDYLDPNGvdkrFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 200 --NSSGTDAFLGTLPFSYsAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVDVNA-DVSSGADIANFVSGSTPMML 276
Cdd:cd14749  161 llGAQGGHWYFQYLVRQA-GGGPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFeGIDYDDAGQAFAQGKAAMNI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 277 QGPTAVSQINElGGDGFesKYATVILPSMNESSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDL 356
Cdd:cd14749  240 GGSWDLGAIKA-GEPGG--KIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLL 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736880152 357 PASQKAWDEDALSGNDKLAAFGDQLKNTMAPPAL-STWAQVSSVADRILEQINKGQVSVDEGLKNLQSEADS 427
Cdd:cd14749  317 PAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLdEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 51-425 3.57e-40

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: 147.14  E-value: 3.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWA--MGNEGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDL-----------AQMGttWMADFS 117
Cdd:cd13657    2 ITIWHalTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLfiwahdwigqfAEAG--LLVPIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 118 NSFSTVpdnlDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIagmagWNKAPKTWNELKRMAKDMQKVDGVKYGM 197
Cdd:cd13657   80 DYLSED----DFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKAL-----VDQPPETTDELLAIMKDHTDPAAGSYGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 198 SLNSSgtDAFLGTlPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFttslYRDGIVD-VNADVSSGADIANFVSGSTPMML 276
Cdd:cd13657  151 AYQVS--DAYFVS-AWIFGFGGYYFDDETDKPGLDTPETIKGIQF----LKDFSWPyMPSDPSYNTQTSLFNEGKAAMII 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 277 QGPTAVSQINELGGDgfeskYATVILPSMNESSGPATsFVG--GCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSS 354
Cdd:cd13657  224 NGPWFIGGIKAAGID-----LGVAPLPTVDGTNPPRP-YSGveGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENG 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736880152 355 DLPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQVSVDEGLKNLQSEA 425
Cdd:cd13657  298 YVPAATNAYDDAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 50-425 1.76e-38

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: 142.43  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  50 DLTIW-AMGNEGDLLDDFVKGFEKENpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMADFSNS--FSTVPDN 126
Cdd:cd13586    1 TITVWtDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAglLAPIPEY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 127 LD-MSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGmagwnKAPKTWNELKRMAKDMQKVDGVKYGMSLNssGTD 205
Cdd:cd13586   80 LAvKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVP-----EPPKTWEELIALAKKFNDKAGGKYGFAYD--QTN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 206 AFLgTLPFSYSAGASL---TNEEQTKWTFDDNGIKKGLNFTTSLYR-DGIVDVNADvSSGADiANFVSGSTPMMLQGPTA 281
Cdd:cd13586  153 PYF-SYPFLAAFGGYVfgeNGGDPTDIGLNNEGAVKGLKFIKDLKKkYKVLPPDLD-YDIAD-ALFKEGKAAMIINGPWD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 282 VSQINELGGDgfeskYATVILPSMNESsGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSDLPASQK 361
Cdd:cd13586  230 LADYKDAGIN-----FGVAPLPTLPGG-KQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKD 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736880152 362 AWDEDALSGNDKLAAFGDQLKNTMAPPALStwaQVSSVADRILEQINK---GQVSVDEGLKNLQSEA 425
Cdd:cd13586  304 ALNDAAVKNDPLVKAFAEQAQYGVPMPNIP---EMAAVWDAMGNALNLvasGKATPEEAAKDAVAAI 367
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 51-425 3.09e-31

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: 122.91  E-value: 3.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWAMGNEGDL--LDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDL-----------AQMGttWMADFS 117
Cdd:cd13522    2 ITVWHQYDTGENqaVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVvfgpsdslgpfAAAG--LLAPLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 118 NSFStvPDNLDMSDFSDGSRatgqVDGKQLGVPWYIDTRVLYYRTDIAGmagwNKAPKTWNELKRMAKDMQKVDgvKYGM 197
Cdd:cd13522   80 EYVS--KSGKYAPNTIAAMK----LNGKLYGVPVSVGAHLMYYNKKLVP----KNPPKTWQELIALAQGLKAKN--VWGL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 198 SLNssGTDAFLgTLPFSYSAGASLTNEEQTKW--TFDDNGIKKGLNFTTSL-YRDGIVDVNADvSSGADiANFVSGSTPM 274
Cdd:cd13522  148 VYN--QNEPYF-FAAWIGGFGGQVFKANNGKNnpTLDTPGAVEALQFLVDLkSKYKIMPPETD-YSIAD-ALFKAGKAAM 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 275 MLQGPTAVSQINELGGDgfesKYATVILPSMNESSGPATsFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSS 354
Cdd:cd13522  223 IINGPWDLGDYRQALKI----NLGVAPLPTFSGTKHAAP-FVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAG 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736880152 355 DLPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALstwAQVSSVADRILEQINK---GQVSVDEGLKNLQSEA 425
Cdd:cd13522  298 DIPANLQAYESPAVQNKPAQKASAEQAAYGVPMPNI---PEMRAVWDAFRIAVNSvlaGKVTPEAAAKDAQQEA 368
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 51-420 3.98e-30

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: 119.90  E-value: 3.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  51 LTIWA-MGNEGDLLDDFVKGFEKENpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLaqmgTTWMADFSNSFST------- 122
Cdd:cd13658    2 LTVWVdEDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDV----MVAPHDRIGSAVLqgllspi 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 123 VPDNLDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGmagwnKAPKTWNELKRMAKDMQKVDGVKYGMSLNSs 202
Cdd:cd13658   77 KLSKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVK-----NAPKTFDELEALAKDLTKEKGKQYGFLADA- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 203 gtDAFLGTLPFSYSAGASLTNEEQTKWTFDDNGIK-----KGLNFTTSLYRDGIV--DVNADVSSGAdianFVSGSTPMM 275
Cdd:cd13658  151 --TNFYYSYGLLAGNGGYIFKKNGSDLDINDIGLNspgavKAVKFLKKWYTEGYLpkGMTGDVIQGL----FKEGKAAAV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 276 LQGPTAVSQINELGGDgfeskYATVILPSMNESSgPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSD 355
Cdd:cd13658  225 IDGPWAIQEYQEAGVN-----YGVAPLPTLPNGK-PMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNE 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736880152 356 LPAsQKAWDEDALSGNDKLA-AFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQVSVDEGLKN 420
Cdd:cd13658  299 IPP-RKDVRSDPEIKNNPLTsAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALND 363
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 59-347 6.14e-30

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: 117.52  E-value: 6.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152   59 EGDLLDDFVKGFEKENPDVKIKVTAIPWSSAHDKLQTAIAAGNGP-DLAQMGTTWMADFSNsfSTVPDNLDmsdfSDGSR 137
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK--AGLLLPLD----DYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  138 ATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGwNKAPKTWNELKRMAKDMQKVDGVKYGMSLNSSGTDAFLGTLPFSYSA 217
Cdd:pfam01547  80 YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAG-LDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLASL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  218 GASLTNEEQ----TKWTFDDNGIKKGLNFTTSLYRDGIVDVNADVSSGADIANFVSGSTPMMLQGPTAVSQIN--ELGGD 291
Cdd:pfam01547 159 GGPLFDKDGggldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANkvKLKVA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 736880152  292 GFESKYATVILPSMNESSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQA 347
Cdd:pfam01547 239 FAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 65-369 3.68e-28

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 112.50  E-value: 3.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152   65 DFVKGFEKENpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLA--QMGTTWMADFSNSFSTVP-DNLDMSDFSDGSRATGQ 141
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDvvWIAADQLATLAEAGLLADlSDVDNLDDLPDALDAAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  142 VDGKQLGVPWYIDT-RVLYYRTDIAGMAGwnKAPKTWNELKRMAKDMQKvdgvKYGMSLNSSGTDAFlgtlpFSYSAGAS 220
Cdd:pfam13416  80 YDGKLYGVPYAASTpTVLYYNKDLLKKAG--EDPKTWDELLAAAAKLKG----KTGLTDPATGWLLW-----ALLADGVD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  221 LTNEEQTKwtfddNGIKKGLNFTTSLYRDGIVdvnadVSSGAD-IANFVSGSTPMMLQGPTAVSQINELGGdgfesKYAT 299
Cdd:pfam13416 149 LTDDGKGV-----EALDEALAYLKKLKDNGKV-----YNTGADaVQLFANGEVAMTVNGTWAAAAAKKAGK-----KLGA 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736880152  300 VILPSmnessgpaTSFVGGCNLVTFKDSKNKQ-SAWKFIQWASKPEVQAEWYKKSSDLPASQKAWDEDALS 369
Cdd:pfam13416 214 VVPKD--------GSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVK 276
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 50-384 4.04e-15

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: 76.23  E-value: 4.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  50 DLTIWAMGNEGDLLDDFVKGFEKENPDVKIKVTAIPWSS--AHDKLQT---------AIAAGNGPDLAQMGTtwMADFSN 118
Cdd:cd13655    1 TLTVWGPQEDQEWLKEMVDAFKEKHPEWKITITIGVVGEadAKDEVLKdpsaaadvfAFANDQLGELVDAGA--IYPLTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 119 SFSTVPDNLDmsdfSDGSRATGQVDGKQLGVPWYIDTRVLYYrtdiagmagwNKAPKTWNELKRMAKDMQKVDGV--KYG 196
Cdd:cd13655   79 SAVDKIKNTN----SEATVDAVTYNGKLYGYPFTANTWFMYY----------DKSKLTEDDVKSLDTMLAKAPDAkgKVS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 197 MSLNSSgtdAFLGtlPFSYSAGASLTNEEQTKWTFDDNGIKKGLNFTTSLYrdGIVDVNA--DVSSGADIANFVSGSTPM 274
Cdd:cd13655  145 FDLSNS---WYLY--AFFFGAGCKLFGNNGGDTAGCDFNNEKGVAVTNYLV--DLVANPKfvNDADGDAISGLKDGTLGA 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 275 MLQGPTAVSQINELGGDGfeskYATVILPSMNESSG--PATSFVG----GCNLVTfkdsKNKQSAWKFIQWASKPEVQAE 348
Cdd:cd13655  218 GVSGPWDAANLKKALGDN----YAVAKLPTYTLGGKdvQMKSFAGykaiGVNSNT----KNPEAAMALADYLTNEESQLT 289

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 736880152 349 WYKKSSDLPASQKAWDEDALSGNDKLAAFGDQLKNT 384
Cdd:cd13655  290 RFEKRGIGPTNKEAAESDAVKADPAAKALIAQSNEA 325
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 49-423 1.76e-14

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: 74.55  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  49 GDLTIWAMGNEG-DLLDDFVKGFEKenpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLaqmgTTWMADFSNSFSTV---- 123
Cdd:cd13656    1 GKLVIWINGDKGyNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDI----IFWAHDRFGGYAQSglla 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 124 ---PDNLDMSDFSDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAgmagwNKAPKTWNELKRMAKDMQKVDGVKYGMSLN 200
Cdd:cd13656   74 eitPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDKELKAKGKSALMFNLQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 201 SSgtdafLGTLPFSYSAGASLTNEEQTKWTFDDNGI-----KKGLNFTTSLYRDGIVDVNADVSSGAdiANFVSGSTPMM 275
Cdd:cd13656  149 EP-----YFTWPLIAADGGYAFKYENGKYDIKDVGVdnagaKAGLTFLVDLIKNKHMNADTDYSIAE--AAFNKGETAMT 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 276 LQGPTAVSQINELGGDgfeskYATVILPSMneSSGPATSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAEWYKKSSD 355
Cdd:cd13656  222 INGPWAWSNIDTSKVN-----YGVTVLPTF--KGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP 294

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736880152 356 LPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQVSVDEGLKNLQS 423
Cdd:cd13656  295 LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT 362
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
49-338 3.21e-12

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 67.73  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  49 GDLTIWAMGNEG-DLLDDFVKGFEKenpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDL-----------AQMG----TTW 112
Cdd:PRK09474  31 GKLVIWINGDKGyNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDIifwahdrfggyAQSGllaeVTP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 113 MADFSNSFStvpdnldmsDFS-DGSRatgqVDGKQLGVPWYIDTRVLYYRTDIAgmagwNKAPKTWNELKRMAKDMQKvD 191
Cdd:PRK09474 108 SKAFKDKLV---------PFTwDAVR----YNGKLIGYPIAVEALSLIYNKDLV-----PTPPKTWEEIPALDKELKA-K 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 192 GvKYGMSLNSSGTdAFlgTLPFSYSAGASLTNEEQTKWTFDDNGI-----KKGLNFTTSLYRDGIVDVNADVSSGAdiAN 266
Cdd:PRK09474 169 G-KSAIMWNLQEP-YF--TWPLIAADGGYAFKFENGGYDVKDVGVnnagaKAGLQFLVDLVKNKHMNADTDYSIAE--AA 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736880152 267 FVSGSTPMMLQGPTAVSQINELGGDgfeskYATVILPSMNesSGPATSFVG----GCNLVtfkdSKNKQSAWKFIQ 338
Cdd:PRK09474 243 FNKGETAMTINGPWAWSNIDKSGIN-----YGVTVLPTFN--GKPSKPFVGvlsaGINAA----SPNKELAKEFLE 307
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 72-430 5.05e-12

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: 67.35  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  72 KENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQ-MGTTWMADFSNS--FSTVPDNLD------MSDFSDGSRATGQV 142
Cdd:cd13580   29 EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQgaLWDLTDYLDkyypnlKKIIEQEGWDSASV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 143 DGKQLGVPW---YIDTRVLYYRTDI---AGMagwnKAPKTWNELKRMAK-----DMQKvDGVK--YGMslnssgTDAFLG 209
Cdd:cd13580  109 DGKIYGIPRkrpLIGRNGLWIRKDWldkLGL----EVPKTLDELYEVAKaftekDPDG-NGKKdtYGL------TDTKDL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 210 TLPFSYSAGASLTNEEQTKWTFDDNGI---------KKGLNFTTSLYRDGIVD----VNADVSSGADIANFVSGSTPMML 276
Cdd:cd13580  178 IGSGFTGLFGAFGAPPNNWWKDEDGKLvpgsiqpemKEALKFLKKLYKEGLIDpefaVNDGTKANEKFISGKAGIFVGNW 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 277 QGPTAVSQINELGGDGFESKYATVILPSMNESSGPATSFVGGCNLVTfKDSKNKQSAWKFIQWASKPEVQ--AEWYKK-- 352
Cdd:cd13580  258 WDPAWPQASLKKNDPDAEWVAVPIPSGPDGKYGVWAESGVNGFFVIP-KKSKKPEAILKLLDFLSDPEVQklLDYGIEgv 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 353 ----------SSDLPASQKAWDEDALSGNDKLAAFGDQLKNTMAPPALSTWAQVSSVADRILEQINKGQvSVDEGLKNLQ 422
Cdd:cd13580  337 hytvkdggpvNIIPPDKQEVGDATLDYFQGSLALEKYKLTNNGERKSDAKKEALDERVVNANDEENENI-AVGPPTETLV 415


                 ....*...
gi 736880152 423 SEADSIGT 430
Cdd:cd13580  416 SPTEKYGA 423
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
44-364 1.22e-09

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 59.81  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  44 SSKATGDLTIW-AMGNE-GDLLDDFVKGFEKENPDVKIkvtaIP-WSSAHDK-LQTAIAA---GNGPDLAQM---GT-TW 112
Cdd:PRK10974  21 NAQAVTEIPFWhSMEGElGKEVDSLAQRFNASQPDYKI----VPvYKGNYEQsLAAGIAAfrsGNAPAILQVyevGTaTM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 113 MAD-----FSNSFSTVPDNLDMSDF--SDGSRATGQVDGKQLGVPWYIDTRVLYYRTDIAGMAGW--NKAPKTWNELkrm 183
Cdd:PRK10974  97 MASkaikpVYDVFKDAGIPFDESQFvpTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpEQPPKTWQDL--- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 184 AKDMQKVDgvKYGMSLN-SSGTDAFLGTLPFSYSAGASLTNEEQ------TKWTFDDNGIKKGLNFTTSLYRDGivDVNA 256
Cdd:PRK10974 174 AAYAAKLR--AAGMKCGyASGWQGWIQLENFSAWHGLPFASKNNgfdgtdAVLEFNKPEQVKHIALLEEMNKKG--DFTY 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 257 DVSSGADIANFVSGSTPMMLQGPTAVSQINELGgdgfESKYATVILP-SMNESSGPATSFVGGCNL--VTFKDSKNKQSA 333
Cdd:PRK10974 250 VGRKDESTEKFYNGDCAITTASSGSLANIRKYA----KFNYGVGMMPyDADVKGAPQNAIIGGASLwvMQGKDKETYKGV 325

                        330       340       350
                 ....*....|....*....|....*....|.
gi 736880152 334 WKFIQWASKPEVQAEWYKKSSDLPASQKAWD 364
Cdd:PRK10974 326 AKFLDFLAKPENAAEWHQKTGYLPITTAAYD 356
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
44-395 3.39e-09

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 58.00  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  44 SSKATGDLTIWAMGneGDLLDDFVKGFEKENpdvKIKVTAIPWSSAhDKLQTAIAAGNGP-DLAQMGTTWMA-------- 114
Cdd:COG0687   24 AAAAEGTLNVYNWG--GYIDPDVLEPFEKET---GIKVVYDTYDSN-EEMLAKLRAGGSGyDVVVPSDYFVArlikagll 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 115 ---DFSN--SFSTVPDNLDMSDFSDGsratgqvdgKQLGVPWYIDTRVLYYRTDIAGmagwnKAPKTWNELKRmAKDMQK 189
Cdd:COG0687   98 qplDKSKlpNLANLDPRFKDPPFDPG---------NVYGVPYTWGTTGIAYNTDKVK-----EPPTSWADLWD-PEYKGK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 190 VdgvkygmSLNSSGTDAFLGTLpfsYSAGASLTNEeqtkwtfDDNGIKKGLNFTTSLYRdgivDVNADVSSGADIAN-FV 268
Cdd:COG0687  163 V-------ALLDDPREVLGAAL---LYLGYDPNST-------DPADLDAAFELLIELKP----NVRAFWSDGAEYIQlLA 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 269 SGSTPMMLQGPTAVSQINElggDGFESKYATvilPsmneSSGpatSFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQAE 348
Cdd:COG0687  222 SGEVDLAVGWSGDALALRA---EGPPIAYVI---P----KEG---ALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAA 288

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 736880152 349 WYKKSSDLPASQKAWDE--DALSGNDKLAAFGDQLKNTMAPPALSTWAQ 395
Cdd:COG0687  289 LAEYVGYAPPNKAARELlpPELAANPAIYPPEEVLDKLEFWNPLPPENR 337
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 72-355 6.44e-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: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 57.75  E-value: 6.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  72 KENPDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTwmaDFSNSFSTVPDNLDMSDFSD---------------GS 136
Cdd:cd13583   27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVLYP---GEENEFVASGALLPISDYLDympnykkyvekwglgKE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 137 RATG-QVDGKQLGVPWYIDTRV----LYYRTDIAGMAGWnKAPKTWNELKRMAKDMQKVDGVKYGMSLNSSGTDAFLGTL 211
Cdd:cd13583  104 LATGrQSDGKYYSLPGLHEDPGvqysFLYRKDIFEKAGI-KIPTTWDEFYAALKKLKEKYPDSYPYSDRWNSNALLLIAA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 212 P-FSYSAGA----SLTNEEQTKWTF--DDNGIKKGLNFTTSLYRDGIVDVN-ADVSSGADIANFVSGSTPMMLQGPTAVS 283
Cdd:cd13583  183 PaFGTTAGWgfsnYTYDPDTDKFVYgaTTDEYKDMLQYFNKLYAEGLLDPEsFTQTDDQAKAKFLNGKSFVITTNPQTVD 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 284 QINELGGDGFESKYATVILPSMNESSG---PATSFVGGCNL-VTFKDSKNKQSAWKFIQWASKPEVQ--AEW------YK 351
Cdd:cd13583  263 ELQRNLRAADGGNYEVVSITPPAGPAGkaiNGSRLENGFMIsSKAKDSKNFEALLQFLDWLYSDEGQelATWgvegetYT 342


                 ....
gi 736880152 352 KSSD 355
Cdd:cd13583  343 KEGD 346
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 76-346 2.14e-05

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 46.68  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  76 DVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMG---TTWMADF-SNSFSTVPDNLD--------MSDFSDGSRATGQVD 143
Cdd:cd13521   31 NVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADylkDKFIAYGmEGAFLPLSKYIDqypnlkafFKQHPDVLRASTASD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 144 GKQLGVPWYID----TRVLYYRTDIAGMAGWnKAPKTWNELKRMAKDMQKVDGVKYG-----MSLNSSGTDAFLGTLPFs 214
Cdd:cd13521  111 GKIYLIPYEPPkdvpNQGYFIRKDWLDKLNL-KTPKTLDELYNVLKAFKEKDPNGNGkadeiPFIDRDPLYGAFRLINS- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 215 ySAGASLTNEEQTKWTFDDNGIKKglNFTTSLYRDGIVDVNADVSSG---ADIAN---------FVSGSTPMMLQGPTAV 282
Cdd:cd13521  189 -WGARSAGGSTDSDWYEDNGKFKH--PFASEEYKDGMKYMNKLYTEGlidKESFTqkddqaeqkFSNGKLGGFTHNWFAS 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736880152 283 SQINELGGDGFESKYATVILPSmNESSGPAT-----SFVGGCNLVTFKDSKNKQSAWKFIQWASKPEVQ 346
Cdd:cd13521  266 DNLFTAQLGKEKPMYILLPIAP-AGNVKGRReedspGYTGPDGVAISKKAKNPVAALKFFDWLASEEGR 333
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 65-253 3.28e-04

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: 42.69  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152  65 DFVKGFEKENpDVKIKVTAIPWSSAHDKLQTAIAAGNGPDLAQMGTTWMAD-----FSNSFSTVPDNLD---------MS 130
Cdd:cd13581   21 LFFKRLEEKT-GIKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAGASDADlmtygKQGLFLPLEDLIDkyapnlkalFD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 131 DFSDGSRATGQVDGKQLGVPWYI--DTRVLYYRT-------DIAGMagwnKAPKTWNELKRMAKDMQKVDGVKYG----- 196
Cdd:cd13581  100 ENPDIKAAITAPDGHIYALPSVNecYHCSYGQRMwinkkwlDKLGL----EMPTTTDELYEVLKAFKEQDPNGNGkadei 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736880152 197 ----MSLNSSGTD------AFLGTLPFSYSAGAsLTNEEQTKWTFDDNGIKKGLNFTTSLYRDGIVD 253
Cdd:cd13581  176 plsfSGLNGGTDDpafllnSFGINDGGYGGYGF-VVKDGKVIYTATDPEYKEALAYLNKLYKEGLID 241
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 253-357 5.80e-04

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: 41.44  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736880152 253 DVNADVSSGADIAN-FVSGSTPMMLQGPTAVSQINElggDGFESKYAtvilpsMNESSGPATSFVggcnLVTFKDSKNKQ 331
Cdd:cd13589  176 NVVTWWTSGAQLAQlLQSGEVDMAPAWNGRAQALID---AGAPVAFV------WPKEGAILGPDT----LAIVKGAPNKE 242

                         90       100
                 ....*....|....*....|....*.
gi 736880152 332 SAWKFIQWASKPEVQAEWYKKSSDLP 357
Cdd:cd13589  243 LAMKFINFALSPEVQAALAEALGYGP 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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